Regulation of peroxisomal lipid metabolism: The role of acyl-CoA and coenzyme A metabolizing enzymes
Peroxisomes are nearly ubiquitous organelles involved in a number of metabolic pathways that vary between organisms and tissues. A common metabolic function in mammals is the partial degradation of various (di)carboxylic acids via α- and β-oxidation. While only a small number of enzymes catalyze the...
Saved in:
| Published in | Biochimie Vol. 98; pp. 45 - 55 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
France
Elsevier B.V
01.03.2014
|
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | Peroxisomes are nearly ubiquitous organelles involved in a number of metabolic pathways that vary between organisms and tissues. A common metabolic function in mammals is the partial degradation of various (di)carboxylic acids via α- and β-oxidation. While only a small number of enzymes catalyze the reactions of β-oxidation, numerous auxiliary enzymes have been identified to be involved in uptake of fatty acids and cofactors required for β-oxidation, regulation of β-oxidation and transport of metabolites across the membrane. These proteins include membrane transporters/channels, acyl-CoA thioesterases, acyl-CoA:amino acid N-acyltransferases, carnitine acyltransferases and nudix hydrolases. Here we review the current view of the role of these auxiliary enzymes in peroxisomal lipid metabolism and propose that they function in concert to provide a means to regulate fatty acid metabolism and transport of products across the peroxisomal membrane.
•ACOTs, NUDTs and N-acyltransferases regulate peroxisomal coenzyme A metabolism.•Auxiliary enzymes produce metabolites for export out of peroxisomes.•Peroxisomal β-oxidation requires auxiliary enzymes for optimal function.•N-acyl taurines can be synthesized in peroxisomes. |
|---|---|
| AbstractList | Peroxisomes are nearly ubiquitous organelles involved in a number of metabolic pathways that vary between organisms and tissues. A common metabolic function in mammals is the partial degradation of various (di)carboxylic acids via α- and β-oxidation. While only a small number of enzymes catalyze the reactions of β-oxidation, numerous auxiliary enzymes have been identified to be involved in uptake of fatty acids and cofactors required for β-oxidation, regulation of β-oxidation and transport of metabolites across the membrane. These proteins include membrane transporters/channels, acyl-CoA thioesterases, acyl-CoA:amino acid N-acyltransferases, carnitine acyltransferases and nudix hydrolases. Here we review the current view of the role of these auxiliary enzymes in peroxisomal lipid metabolism and propose that they function in concert to provide a means to regulate fatty acid metabolism and transport of products across the peroxisomal membrane. Peroxisomes are nearly ubiquitous organelles involved in a number of metabolic pathways that vary between organisms and tissues. A common metabolic function in mammals is the partial degradation of various (di)carboxylic acids via α- and β-oxidation. While only a small number of enzymes catalyze the reactions of β-oxidation, numerous auxiliary enzymes have been identified to be involved in uptake of fatty acids and cofactors required for β-oxidation, regulation of β-oxidation and transport of metabolites across the membrane. These proteins include membrane transporters/channels, acyl-CoA thioesterases, acyl-CoA:amino acid N-acyltransferases, carnitine acyltransferases and nudix hydrolases. Here we review the current view of the role of these auxiliary enzymes in peroxisomal lipid metabolism and propose that they function in concert to provide a means to regulate fatty acid metabolism and transport of products across the peroxisomal membrane. •ACOTs, NUDTs and N-acyltransferases regulate peroxisomal coenzyme A metabolism.•Auxiliary enzymes produce metabolites for export out of peroxisomes.•Peroxisomal β-oxidation requires auxiliary enzymes for optimal function.•N-acyl taurines can be synthesized in peroxisomes. |
| Author | Alexson, Stefan E.H. Tillander, Veronika Hunt, Mary C. |
| Author_xml | – sequence: 1 givenname: Mary C. surname: Hunt fullname: Hunt, Mary C. email: mary.hunt@dit.ie organization: Dublin Institute of Technology, College of Sciences & Health, School of Biological Sciences, Kevin Street, Dublin 8, Ireland – sequence: 2 givenname: Veronika surname: Tillander fullname: Tillander, Veronika organization: Karolinska Institutet, Department of Laboratory Medicine, Division of Clinical Chemistry, Karolinska University Hospital, SE 141 86, Stockholm, Sweden – sequence: 3 givenname: Stefan E.H. surname: Alexson fullname: Alexson, Stefan E.H. organization: Karolinska Institutet, Department of Laboratory Medicine, Division of Clinical Chemistry, Karolinska University Hospital, SE 141 86, Stockholm, Sweden |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24389458$$D View this record in MEDLINE/PubMed http://kipublications.ki.se/Default.aspx?queryparsed=id:128329849$$DView record from Swedish Publication Index |
| BookMark | eNp9kc1u1DAURi1URKeFN0DISzYJ1z8xDguk0QgKUiUkVNaW7dxpPSRxiJPC9OnrUabDCla2rs7xZ93vgpz1sUdCXjMoGTD1ble6EP1dKDkwUTJeAtPPyIopoQvFtDgjKxAARQ1anpOLlHYAUAGvX5BzLoWuZaVXpPmOt3NrpxB7Grd0wDH-CSl2tqVtGEJDO5ysi21I3Qd6c4d0jC0eSOv3bbGJa2r7hvqI_cO-Q7o-8Q-hv6XLNL0kz7e2TfjqeF6SH58_3Wy-FNffrr5u1teFr5iaCskE8lqjY1ArsLLyUjjPBGiFzEtttfMcsFIgrATpOfeMOe0byZV37ytxSYrl3fQbh9mZYQydHfcm2mCOo5_5hqbisqpV5ut_8sMYm7_Sk8i4FvmLss7u28XN4K8Z02S6kDy2re0xzsmwKu-dS6lFRuWC-jGmNOL2FMTAHLo0O7N0aQ5d5hCTu8zam2PC7DpsTtJTeRn4uACYd3ofcDTJB-w9NmFEP5kmhv8nPAL0z7Sy |
| CitedBy_id | crossref_primary_10_3389_fphys_2020_580167 crossref_primary_10_1002_pros_24027 crossref_primary_10_1194_jlr_M092676 crossref_primary_10_1099_mic_0_000850 crossref_primary_10_1021_acs_jmedchem_9b01463 crossref_primary_10_1074_jbc_M115_651737 crossref_primary_10_1124_jpet_116_233312 crossref_primary_10_1111_jcmm_12481 crossref_primary_10_1007_s10545_015_9819_7 crossref_primary_10_1007_s00018_021_03869_9 crossref_primary_10_1016_j_aquaculture_2023_740095 crossref_primary_10_1021_acs_est_6b03456 crossref_primary_10_1080_01652176_2017_1354561 crossref_primary_10_1111_tpj_13818 crossref_primary_10_1083_jcb_201608128 crossref_primary_10_1016_j_freeradbiomed_2019_12_025 crossref_primary_10_3390_ijms21239057 crossref_primary_10_1111_jnc_16032 crossref_primary_10_1016_j_bbamcr_2015_08_011 crossref_primary_10_1021_acs_jafc_4c00002 crossref_primary_10_1002_pmic_201400280 crossref_primary_10_1111_nph_12809 crossref_primary_10_1016_j_chembiol_2020_12_009 crossref_primary_10_1002_1873_3468_13974 crossref_primary_10_1016_j_bbrc_2018_01_153 crossref_primary_10_3389_fneur_2022_886246 crossref_primary_10_1016_j_plipres_2020_101028 crossref_primary_10_1016_j_gendis_2023_03_019 crossref_primary_10_1002_gepi_22437 crossref_primary_10_1042_BST20140176 crossref_primary_10_1038_s41598_021_95214_0 crossref_primary_10_5551_jat_28720 crossref_primary_10_1152_physrev_00051_2021 crossref_primary_10_1074_jbc_M115_702597 crossref_primary_10_1016_j_bbalip_2018_05_008 crossref_primary_10_1016_j_biochi_2019_10_004 crossref_primary_10_1016_j_plipres_2016_06_002 crossref_primary_10_1038_s41419_018_0406_3 crossref_primary_10_1371_journal_pone_0152877 crossref_primary_10_1038_s41467_021_27738_y crossref_primary_10_1186_s13104_015_1314_6 crossref_primary_10_3389_fcell_2020_00144 crossref_primary_10_1016_j_biopha_2019_109558 crossref_primary_10_1038_s41598_017_06511_6 crossref_primary_10_4014_jmb_2205_05029 crossref_primary_10_1074_jbc_RA117_001358 crossref_primary_10_1002_rcm_6958 crossref_primary_10_1038_s41598_022_21466_z crossref_primary_10_1186_s43008_023_00127_4 crossref_primary_10_1016_j_molmet_2020_01_005 crossref_primary_10_1038_s41598_020_72900_z crossref_primary_10_18632_aging_204803 crossref_primary_10_1016_j_tem_2017_03_001 crossref_primary_10_3892_ol_2017_6594 crossref_primary_10_3390_biomedicines10020216 crossref_primary_10_1038_s42255_024_01059_y crossref_primary_10_1016_j_jbc_2022_102745 crossref_primary_10_1002_1873_3468_13392 crossref_primary_10_1016_j_plipres_2015_04_001 crossref_primary_10_3390_biom10081174 crossref_primary_10_1042_BCJ20160164 crossref_primary_10_1194_jlr_S091371 crossref_primary_10_1007_s11356_018_2358_7 |
| Cites_doi | 10.1194/jlr.M300128-JLR200 10.1073/pnas.1218034110 10.1016/j.bbrc.2012.11.026 10.1016/S0021-9258(19)45222-8 10.1016/S0021-9258(17)32178-6 10.1002/pro.417 10.1016/j.jbiosc.2010.05.004 10.1096/fj.06-6919com 10.1016/S0021-9258(18)90661-7 10.1074/jbc.M313863200 10.1111/j.1600-0854.2012.01393.x 10.1093/oxfordjournals.jbchem.a124337 10.1074/jbc.M300987200 10.1016/S0021-9258(19)78086-7 10.1111/j.1432-1033.1984.tb08267.x 10.1007/s00018-005-5463-y 10.1016/S0163-7827(01)00017-0 10.1016/S0021-9258(19)70773-X 10.1074/jbc.M400162200 10.1146/annurev.biochem.74.082803.133450 10.1002/bies.201000097 10.1111/j.1432-1033.1994.tb18870.x 10.1016/j.yexcr.2004.02.029 10.1074/jbc.M309532200 10.1021/pr9004663 10.1186/1479-7364-4-6-411 10.1006/bbrc.1999.1340 10.1096/fj.06-6042com 10.1016/j.bbadis.2011.12.011 10.1007/BF02535514 10.1016/j.bbalip.2013.06.007 10.1074/jbc.M511762200 10.1177/153537020122600204 10.1006/bbrc.1999.0510 10.1083/jcb.150.3.489 10.1007/s11745-011-3639-9 10.1042/bj2620041 10.1042/BST0350865 10.1111/j.1432-1033.1994.tb18926.x 10.1194/jlr.M012153 10.1016/j.lfs.2005.05.019 10.1016/j.plipres.2010.04.001 10.1021/bi702530z 10.1517/17425255.3.2.159 10.1021/bi0608008 10.1074/jbc.M106458200 10.1006/bbrc.2001.6245 10.1186/1471-2105-5-109 10.1074/jbc.274.14.9216 10.1016/S0006-291X(86)80304-7 10.1016/j.prp.2013.02.008 10.1042/bj20030441 10.1016/0020-711X(80)90015-4 10.1042/BJ20050893 10.1042/BJ20050144 10.1111/j.1432-1033.1994.tb18927.x 10.1194/jlr.R900009-JLR200 10.1074/jbc.M703718200 10.1073/pnas.1002862108 10.1074/mcp.M700169-MCP200 10.1042/BJ20111420 10.1124/mol.109.055624 10.1042/0264-6021:3570033 10.1016/j.plipres.2008.05.001 10.1146/annurev.biochem.74.082803.133329 10.1074/jbc.M508479200 10.1371/journal.pone.0019521 10.1021/bi00272a010 10.1074/jbc.270.9.4908 10.1194/jlr.M030163 10.1016/j.ymgme.2004.08.016 10.1093/oxfordjournals.jbchem.a132918 10.1016/j.bbadis.2012.03.009 10.1016/S0022-2275(20)32139-8 10.1194/jlr.R005959 10.1007/s00018-007-7357-7 10.1385/CBB:32:1-3:01 10.1074/jbc.274.48.34317 10.1093/jb/mvn114 10.1073/pnas.93.24.13748 10.1016/S0021-9258(18)81625-8 10.1016/j.bbalip.2011.06.006 10.1021/bi0480335 10.1016/S0006-291X(02)02663-3 10.1016/j.jchromb.2009.01.002 10.1007/s00018-008-7576-6 10.1074/jbc.M412850200 10.1038/sj.bjp.0706093 10.1016/S0083-6729(09)81008-X 10.1111/j.1476-5381.2011.01435.x 10.1042/bst0280946 10.1006/bbrc.1997.7217 10.1016/j.bbrc.2007.03.083 |
| ContentType | Journal Article |
| Copyright | 2014 Elsevier Masson SAS Copyright © 2014 Elsevier Masson SAS. All rights reserved. |
| Copyright_xml | – notice: 2014 Elsevier Masson SAS – notice: Copyright © 2014 Elsevier Masson SAS. All rights reserved. |
| DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 ADTPV AOWAS |
| DOI | 10.1016/j.biochi.2013.12.018 |
| DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic SwePub SwePub Articles |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic |
| DatabaseTitleList | MEDLINE MEDLINE - Academic |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Engineering Anatomy & Physiology Chemistry |
| EISSN | 1638-6183 |
| EndPage | 55 |
| ExternalDocumentID | oai_swepub_ki_se_524596 oai_prod_swepub_kib_ki_se_128329849 10_1016_j_biochi_2013_12_018 24389458 S0300908413004689 |
| Genre | Research Support, Non-U.S. Gov't Journal Article Review |
| GroupedDBID | --- --K --M -~X .GJ .~1 0R~ 1B1 1RT 1~. 1~5 23N 4.4 457 4G. 53G 5GY 5VS 6J9 7-5 71M 8P~ 9JM AABNK AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AAXUO ABFNM ABFRF ABGSF ABJNI ABMAC ABUDA ABXDB ABYKQ ACDAQ ACGFO ACGFS ACIUM ACRLP ADBBV ADEZE ADMUD ADUVX AEBSH AEFWE AEHWI AEKER AENEX AFKWA AFTJW AFXIZ AGHFR AGRDE AGUBO AGYEJ AHHHB AI. AIEXJ AIKHN AITUG AJBFU AJOXV ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC CS3 DOVZS DU5 EBS EFJIC EFLBG EJD EO8 EO9 EP2 EP3 F5P FDB FEDTE FGOYB FIRID FNPLU FYGXN G-2 G-Q GBLVA HLW HVGLF HZ~ H~9 IHE J1W KOM LX3 M41 MO0 N9A O-L O9- OAUVE OZT P-8 P-9 P2P PC. Q38 R2- RIG ROL RPZ SBG SCC SDF SDG SDP SES SEW SSU SSZ T5K TWZ VH1 WUQ Y6R ZGI ZXP ~02 ~G- ~KM AAHBH AAXKI AFJKZ AKRWK CGR CUY CVF ECM EIF NPM AAYXX ACRPL CITATION 7X8 ADTPV AOWAS ABWVN ADNMO |
| ID | FETCH-LOGICAL-c516t-413e298eb10960a45c43bc13086e1c48a8bc20e5603a404c22c11b8cd426cb753 |
| IEDL.DBID | AIKHN |
| ISSN | 0300-9084 1638-6183 |
| IngestDate | Mon Dec 16 03:37:11 EST 2024 Wed Oct 30 05:07:53 EDT 2024 Fri Oct 25 06:39:11 EDT 2024 Fri Dec 06 02:51:46 EST 2024 Sat Nov 02 12:28:51 EDT 2024 Fri Feb 23 02:29:12 EST 2024 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Keywords | DMN-CoA NAT FAAH AMP Nudix hydrolase β-Oxidation FMN PTS1 CoASH CROT ACNAT BAAT ADP Acyl-CoA:amino acid N-acyltransferase NUDT PPAR Acyl-CoA thioesterase Coenzyme A ACOT Peroxisomal lipid metabolism ACOX3 CRAT PAP |
| Language | English |
| License | Copyright © 2014 Elsevier Masson SAS. All rights reserved. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c516t-413e298eb10960a45c43bc13086e1c48a8bc20e5603a404c22c11b8cd426cb753 |
| Notes | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
| PMID | 24389458 |
| PQID | 1508424483 |
| PQPubID | 23479 |
| PageCount | 11 |
| ParticipantIDs | swepub_primary_oai_swepub_ki_se_524596 swepub_primary_oai_prod_swepub_kib_ki_se_128329849 proquest_miscellaneous_1508424483 crossref_primary_10_1016_j_biochi_2013_12_018 pubmed_primary_24389458 elsevier_sciencedirect_doi_10_1016_j_biochi_2013_12_018 |
| PublicationCentury | 2000 |
| PublicationDate | 2014-03-01 |
| PublicationDateYYYYMMDD | 2014-03-01 |
| PublicationDate_xml | – month: 03 year: 2014 text: 2014-03-01 day: 01 |
| PublicationDecade | 2010 |
| PublicationPlace | France |
| PublicationPlace_xml | – name: France |
| PublicationTitle | Biochimie |
| PublicationTitleAlternate | Biochimie |
| PublicationYear | 2014 |
| Publisher | Elsevier B.V |
| Publisher_xml | – name: Elsevier B.V |
| References | van Roermund, Tabak, van Den Berg, Wanders, Hettema (bib26) 2000; 150 Tilton, Shockey, Browse (bib46) 2000; 28 Prass, Isohashi, Utter (bib57) 1980; 255 Speijer (bib2) 2011; 33 Antonenkov, Hiltunen (bib83) 2012; 1822 Hunt, Solaas, Kase, Alexson (bib39) 2002; 277 Thorsell, Lee, Persson, Siponen, Nilsson, Busam, Kotenvova, Schúler, Lehtió (bib64) 2011; 6 Saghatelian, McKinney, Bandell, Patapoutian, Cravatt (bib74) 2006; 45 Chu, Varanasi, Chu, Lin, Usuda, Rao, Reddy (bib18) 1995; 270 Jones, Nau, Geraghty, Erdmann, Gould (bib48) 1999; 274 Osumi, Hashimoto, Ui (bib17) 1980; 87 Wanders (bib5) 2004; 83 Westin, Hunt, Alexson (bib24) 2005; 280 Baumgart, Vanhooren, Fransen, Marynen, Puype, Vanderkerckhove, Leunissen, Fahimi, Mannaerts, Van Veldhoven (bib36) 1996; 93 Maeda, Delessert, Hasegawa, Seto, Zuber, Poirier (bib55) 2006; 281 Violante, Ijlst, Te Brinke, Koster, Tavares de Almeida, Wanders, Ventura, Houten (bib56) 2013; 1831 Leighton, Bergseth, Rørtveit, Christiansen, Bremer (bib65) 1989; 264 Bian, Kasumov, Thomas, Jobbins, David, Minkler, Hoppel, Brunengraber (bib21) 2005; 280 Le Bon, Cravedi, Tulliez (bib42) 1988; 23 Gasmi, McLennan (bib88) 2001; 357 Westin, Alexson, Hunt (bib23) 2004; 279 Agrimi, Russo, Scarcia, Palmieri (bib84) 2012; 443 Reszko, Kasumov, David, Jobbins, Thomas, Hoppel, Brunengraber, Des Rosiers (bib20) 2004; 279 Jung, Kim, Ryu, Kim, Shin, Kim, Kim (bib53) 2013; 209 Long, LaCava, Jin, Cravatt (bib76) 2011; 52 Croes, Casteels, Dieuaide-Noubhani, Mannaerts, van Veldhoven (bib37) 1999; 40 Ofman, el Mrabet, Dacremont, Spijer, Wanders (bib40) 2002; 290 Nakanishi, Okamoto, Isohashi (bib61) 1994; 115 He, Barnes, Falany (bib96) 2003; 44 Wanders, Waterham (bib4) 2006; 75 Turman, Kingsley, Rouzer, Cravatt, Marnett (bib78) 2008; 47 Faust, Verma, Peng, McNew (bib43) 2012; 13 Steinberg, Wang, Kim, Mihalik, Watkins (bib27) 1999; 257 van Veldhoven, van Rompuy, Fransen, De Béthune, Mannaerts (bib35) 1994; 222 Hunt, Nousiainen, Huttunen, Orii, Svensson, Alexson (bib16) 1999; 274 Reilly, O'Shea, Andersson, O'Byrne, Alexson, Hunt (bib66) 2007; 21 Hunt, Alexson (bib10) 2008; 47 Gachon, Leuenberger, Claudel, Gos, Jouffe, Fleury Olela, de Mollerat du Jeu, Wahli, Schibler (bib93) 2011; 108 Cantu, Chen, Reilly (bib7) 2010; 19 Waluk, Vielfort, Derakhshan, Aro, Hunt (bib80) 2013; 430 Visser, van Roermund, Waterham, Wanders (bib85) 2002; 299 Farrell, Fiol, Reddy, Bieber (bib28) 1984; 259 Isohashi, Nakanishi, Sakamoto (bib62) 1983; 22 Van Veldhoven, Mannaerts (bib50) 1986; 139 Kasumov, Adams, Bian, David, Thomas, Jobbins, Minkler, Hoppel, Brunengraber (bib22) 2005; 389 Dillon, Bateman (bib6) 2004; 5 Osmundsen, Neat, Borrebaek (bib19) 1980; 12 Wanders, Komen, Ferdinandusse (bib30) 2011; 1811 Ferdinandusse, Mulders, IJlst, Denis, Dacremont, Waterham, Wanders (bib41) 1999; 263 Tan, Yu, Monn, Hughes, O'Dell, Walker (bib75) 2009; 877 Visser, van Roermund, Ijlst, Waterham, Wanders (bib91) 2007; 357 van den Brink, Wanders (bib31) 2006; 63 AbdelRaheim, Spiller, McLennan (bib89) 2003; 374 McKinney, Cravatt (bib77) 2005; 74 Himms-Hagen, Harper (bib94) 2001; 226 Knights, Sykes, Miners (bib92) 2007; 3 O'Byrne, Hunt, Rai, Saeki, Alexson (bib70) 2003; 278 Chatzakos, Slätis, Djureinovic, Helleday, Hunt (bib82) 2012; 47 Bonner, Bloch (bib44) 1972; 247 Hunt, Siponen, Alexson (bib11) 2012; 1822 Wilcke, Alexson (bib14) 1994; 222 Brocker, Carpenter, Nebert, Vasiliou (bib12) 2010; 4 Gabaldón (bib1) 2013 Horibata, Ando, Itoh, Sugimoto (bib60) 2013; 54 Reilly, Tillander, Ofman, Alexson, Hunt (bib90) 2008; 144 Wanders, Komen (bib3) 2007; 35 Kemp, Theodoulou, Wanders (bib86) 2011; 164 Ofman, Speijer, Leen, Wanders (bib87) 2006; 393 Wiese, Gronemeyer, Ofman, Kunze, Grou, Almeida, Eisenacher, Stephan, Hayen, Schollenberger, Korosec, Waterham, Schliebs, Erdmann, Berger, Meyer, Just, Azevedo, Wanders, Warscheid (bib58) 2007; 6 Islinger, Li, Loos, Liebler, Angermüller, Eckerskorn, Weber, Abdolzade, Völkl (bib59) 2010; 9 De Marcos, van Roermund, Postis, Dietrich, Kerr, Wanders, Baldwin, Baker, Theodoulou (bib13) 2013; 110 Falany, Johnson, Barnes, Diasio (bib95) 1994; 269 Ishizuka, Toyama, Watanabe, Fujiki, Takeuchi, Yamasaki, Yuasa, Miyazaki, Nakajima, Taki, Saito (bib52) 2004; 297 Hunt, Rautanen, Westin, Svensson, Alexson (bib25) 2006; 20 Zhang, Agarwal, Beylot, Soloviev, David, Reider, Anderson, Tserng, Brunengraber (bib71) 1994; 269 Vriens, Appendino, Nilius (bib79) 2009; 75 Komen, Distelmaier, Koopman, Wanders, Smeitink, Willems (bib33) 2007; 64 Ferdinandusse, Denis, Faust, Wanders (bib69) 2009; 50 Isohashi, Nakanishi, Matsunaga, Sakamoto (bib63) 1984; 142 Kal, Hettema, van den Berg, Koerkamp, van Ijlst, Distel, Tabak (bib51) 2000; 32 Kirkby, Roman, Kobe, Kellie, Forwood (bib8) 2010; 49 Tilton, Shockey, Browse (bib47) 2004; 279 Bradshaw, Rimmerman, Hu, Burstein, Walker (bib67) 2009; 81 Watanabe, Shiratori, Shoji, Miyatake, Okazaki, Ikuta, Sato, Saito (bib49) 1997; 238 Westin, Hunt, Alexson (bib34) 2007; 282 Hunt, Alexson (bib9) 2002; 41 Wu, Qin, Fako, Zhang (bib54) 2013 Saghatelian, Trauger, Want, Hawkins, Siuzdak, Cravatt (bib73) 2004; 43 Westin, Hunt, Alexson (bib29) 2008; 65 Seto, Kang, Ming, Habu, Nihei, Ueda, Maeda (bib45) 2010; 110 Saghatelian, Cravatt (bib72) 2005; 77 Schmitz, Fingerhut, Conzelmann (bib38) 1994; 222 Van Veldhoven (bib32) 2010; 10 Bradshaw, Walker (bib68) 2005; 144 M.O. Roy, S. Hannedouche, Ligand for G-protein Coupled Receptor GPR72 and Uses Thereof, Canadian Patent Application, C. P. Application, editor., 2007, 1–99. Alexson, Osmundsen, Berge (bib15) 1989; 262 Hunt (10.1016/j.biochi.2013.12.018_bib39) 2002; 277 Prass (10.1016/j.biochi.2013.12.018_bib57) 1980; 255 Chatzakos (10.1016/j.biochi.2013.12.018_bib82) 2012; 47 Kemp (10.1016/j.biochi.2013.12.018_bib86) 2011; 164 Isohashi (10.1016/j.biochi.2013.12.018_bib62) 1983; 22 Westin (10.1016/j.biochi.2013.12.018_bib34) 2007; 282 Wanders (10.1016/j.biochi.2013.12.018_bib5) 2004; 83 Thorsell (10.1016/j.biochi.2013.12.018_bib64) 2011; 6 Waluk (10.1016/j.biochi.2013.12.018_bib80) 2013; 430 Visser (10.1016/j.biochi.2013.12.018_bib85) 2002; 299 O'Byrne (10.1016/j.biochi.2013.12.018_bib70) 2003; 278 Agrimi (10.1016/j.biochi.2013.12.018_bib84) 2012; 443 van Roermund (10.1016/j.biochi.2013.12.018_bib26) 2000; 150 Horibata (10.1016/j.biochi.2013.12.018_bib60) 2013; 54 Ferdinandusse (10.1016/j.biochi.2013.12.018_bib41) 1999; 263 Westin (10.1016/j.biochi.2013.12.018_bib23) 2004; 279 Wilcke (10.1016/j.biochi.2013.12.018_bib14) 1994; 222 Wanders (10.1016/j.biochi.2013.12.018_bib4) 2006; 75 Reilly (10.1016/j.biochi.2013.12.018_bib66) 2007; 21 Watanabe (10.1016/j.biochi.2013.12.018_bib49) 1997; 238 Westin (10.1016/j.biochi.2013.12.018_bib29) 2008; 65 Knights (10.1016/j.biochi.2013.12.018_bib92) 2007; 3 Leighton (10.1016/j.biochi.2013.12.018_bib65) 1989; 264 Zhang (10.1016/j.biochi.2013.12.018_bib71) 1994; 269 Brocker (10.1016/j.biochi.2013.12.018_bib12) 2010; 4 Kal (10.1016/j.biochi.2013.12.018_bib51) 2000; 32 Saghatelian (10.1016/j.biochi.2013.12.018_bib74) 2006; 45 Gabaldón (10.1016/j.biochi.2013.12.018_bib1) 2013 Kirkby (10.1016/j.biochi.2013.12.018_bib8) 2010; 49 Gasmi (10.1016/j.biochi.2013.12.018_bib88) 2001; 357 Bradshaw (10.1016/j.biochi.2013.12.018_bib67) 2009; 81 Cantu (10.1016/j.biochi.2013.12.018_bib7) 2010; 19 Chu (10.1016/j.biochi.2013.12.018_bib18) 1995; 270 Baumgart (10.1016/j.biochi.2013.12.018_bib36) 1996; 93 Ofman (10.1016/j.biochi.2013.12.018_bib87) 2006; 393 Ishizuka (10.1016/j.biochi.2013.12.018_bib52) 2004; 297 Saghatelian (10.1016/j.biochi.2013.12.018_bib72) 2005; 77 Turman (10.1016/j.biochi.2013.12.018_bib78) 2008; 47 Steinberg (10.1016/j.biochi.2013.12.018_bib27) 1999; 257 Croes (10.1016/j.biochi.2013.12.018_bib37) 1999; 40 Isohashi (10.1016/j.biochi.2013.12.018_bib63) 1984; 142 Speijer (10.1016/j.biochi.2013.12.018_bib2) 2011; 33 Long (10.1016/j.biochi.2013.12.018_bib76) 2011; 52 Hunt (10.1016/j.biochi.2013.12.018_bib11) 2012; 1822 Visser (10.1016/j.biochi.2013.12.018_bib91) 2007; 357 Kasumov (10.1016/j.biochi.2013.12.018_bib22) 2005; 389 Wiese (10.1016/j.biochi.2013.12.018_bib58) 2007; 6 Osmundsen (10.1016/j.biochi.2013.12.018_bib19) 1980; 12 Hunt (10.1016/j.biochi.2013.12.018_bib16) 1999; 274 Bonner (10.1016/j.biochi.2013.12.018_bib44) 1972; 247 Violante (10.1016/j.biochi.2013.12.018_bib56) 2013; 1831 Islinger (10.1016/j.biochi.2013.12.018_bib59) 2010; 9 10.1016/j.biochi.2013.12.018_bib81 Jung (10.1016/j.biochi.2013.12.018_bib53) 2013; 209 McKinney (10.1016/j.biochi.2013.12.018_bib77) 2005; 74 Vriens (10.1016/j.biochi.2013.12.018_bib79) 2009; 75 Tilton (10.1016/j.biochi.2013.12.018_bib47) 2004; 279 He (10.1016/j.biochi.2013.12.018_bib96) 2003; 44 Maeda (10.1016/j.biochi.2013.12.018_bib55) 2006; 281 Antonenkov (10.1016/j.biochi.2013.12.018_bib83) 2012; 1822 Himms-Hagen (10.1016/j.biochi.2013.12.018_bib94) 2001; 226 Wu (10.1016/j.biochi.2013.12.018_bib54) 2013 Hunt (10.1016/j.biochi.2013.12.018_bib9) 2002; 41 Faust (10.1016/j.biochi.2013.12.018_bib43) 2012; 13 AbdelRaheim (10.1016/j.biochi.2013.12.018_bib89) 2003; 374 Osumi (10.1016/j.biochi.2013.12.018_bib17) 1980; 87 Ofman (10.1016/j.biochi.2013.12.018_bib40) 2002; 290 Jones (10.1016/j.biochi.2013.12.018_bib48) 1999; 274 Farrell (10.1016/j.biochi.2013.12.018_bib28) 1984; 259 van Veldhoven (10.1016/j.biochi.2013.12.018_bib35) 1994; 222 Hunt (10.1016/j.biochi.2013.12.018_bib10) 2008; 47 Falany (10.1016/j.biochi.2013.12.018_bib95) 1994; 269 De Marcos (10.1016/j.biochi.2013.12.018_bib13) 2013; 110 Bian (10.1016/j.biochi.2013.12.018_bib21) 2005; 280 Dillon (10.1016/j.biochi.2013.12.018_bib6) 2004; 5 Van Veldhoven (10.1016/j.biochi.2013.12.018_bib32) 2010; 10 Saghatelian (10.1016/j.biochi.2013.12.018_bib73) 2004; 43 Gachon (10.1016/j.biochi.2013.12.018_bib93) 2011; 108 Van Veldhoven (10.1016/j.biochi.2013.12.018_bib50) 1986; 139 Tan (10.1016/j.biochi.2013.12.018_bib75) 2009; 877 Alexson (10.1016/j.biochi.2013.12.018_bib15) 1989; 262 Tilton (10.1016/j.biochi.2013.12.018_bib46) 2000; 28 Reszko (10.1016/j.biochi.2013.12.018_bib20) 2004; 279 Westin (10.1016/j.biochi.2013.12.018_bib24) 2005; 280 Komen (10.1016/j.biochi.2013.12.018_bib33) 2007; 64 Bradshaw (10.1016/j.biochi.2013.12.018_bib68) 2005; 144 Le Bon (10.1016/j.biochi.2013.12.018_bib42) 1988; 23 Wanders (10.1016/j.biochi.2013.12.018_bib30) 2011; 1811 Schmitz (10.1016/j.biochi.2013.12.018_bib38) 1994; 222 Seto (10.1016/j.biochi.2013.12.018_bib45) 2010; 110 Ferdinandusse (10.1016/j.biochi.2013.12.018_bib69) 2009; 50 Nakanishi (10.1016/j.biochi.2013.12.018_bib61) 1994; 115 Reilly (10.1016/j.biochi.2013.12.018_bib90) 2008; 144 Hunt (10.1016/j.biochi.2013.12.018_bib25) 2006; 20 van den Brink (10.1016/j.biochi.2013.12.018_bib31) 2006; 63 Wanders (10.1016/j.biochi.2013.12.018_bib3) 2007; 35 |
| References_xml | – volume: 257 start-page: 615 year: 1999 end-page: 621 ident: bib27 article-title: Human very-long-chain acyl-CoA synthetase: cloning, topography and relevance to branched-chain fatty acid metabolism publication-title: Biochem. Biophys. Res. Commun. contributor: fullname: Watkins – volume: 247 start-page: 3123 year: 1972 end-page: 3133 ident: bib44 article-title: Purification and properties of fatty acyl thioesterase I from publication-title: J. Biol. Chem. contributor: fullname: Bloch – volume: 144 start-page: 459 year: 2005 end-page: 465 ident: bib68 article-title: The expanding field of cannabimimetic and related lipid mediators publication-title: Br. J. Pharmacol. contributor: fullname: Walker – volume: 23 start-page: 424 year: 1988 end-page: 429 ident: bib42 article-title: Disposition and metabolism of pristane in rat publication-title: Lipids contributor: fullname: Tulliez – volume: 269 start-page: 11025 year: 1994 end-page: 11029 ident: bib71 article-title: Nonhomogeneous labeling of liver extra-mitochondrial acetyl-CoA. Implications for the probing of lipogenic acetyl-CoA via drug acetylation and for the production of acetate by the liver publication-title: J. Biol. Chem. contributor: fullname: Brunengraber – volume: 33 start-page: 88 year: 2011 end-page: 94 ident: bib2 article-title: Oxygen radicals shaping evolution: why fatty acid catabolism leads to peroxisomes while neurons do without it: FADH publication-title: BioEssays contributor: fullname: Speijer – volume: 47 start-page: 355 year: 2012 end-page: 361 ident: bib82 article-title: -Acyl taurines are anti-proliferative in prostate cancer cells publication-title: Lipids contributor: fullname: Hunt – volume: 282 start-page: 26707 year: 2007 end-page: 26716 ident: bib34 article-title: Peroxisomes contain a specific phytanoyl-CoA/pristanoyl-CoA thioesterase acting as a novel auxiliary enzyme in alpha- and beta-oxidation of methyl-branched fatty acids in mouse publication-title: J. Biol. Chem. contributor: fullname: Alexson – year: 2013 ident: bib54 article-title: Molecular mechanisms of fatty acid synthase (FASN)-mediated resistance to anti-cancer treatments publication-title: Adv. Biol. Regul. contributor: fullname: Zhang – volume: 277 start-page: 1128 year: 2002 end-page: 1138 ident: bib39 article-title: Characterization of an acyl-CoA thioesterase that functions as a major regulator of peroxisomal lipid metabolism publication-title: J. Biol. Chem. contributor: fullname: Alexson – volume: 83 start-page: 16 year: 2004 end-page: 27 ident: bib5 article-title: Peroxisomes, lipid metabolism, and peroxisomal disorders publication-title: Mol. Genet. Metab. contributor: fullname: Wanders – volume: 47 start-page: 405 year: 2008 end-page: 421 ident: bib10 article-title: Novel functions of acyl-CoA thioesterases and acyltransferases as auxiliary enzymes in peroxisomal lipid metabolism publication-title: Prog. Lipid Res. contributor: fullname: Alexson – volume: 3 start-page: 159 year: 2007 end-page: 168 ident: bib92 article-title: Amino acid conjugation: contribution to the metabolism and toxicity of xenobiotic carboxylic acids publication-title: Expert Opin. Drug Metab. Toxicol. contributor: fullname: Miners – year: 2013 ident: bib1 article-title: A metabolic scenario for the evolutionary origin of peroxisomes from the endomembranous system publication-title: Cell. Mol. Life Sci. contributor: fullname: Gabaldón – volume: 139 start-page: 1195 year: 1986 end-page: 1201 ident: bib50 article-title: Coenzyme A in purified peroxisomes is not freely soluble in the matrix but firmly bound to a matrix protein publication-title: Biochem. Biophys. Res. Commun. contributor: fullname: Mannaerts – volume: 54 start-page: 2049 year: 2013 end-page: 2059 ident: bib60 article-title: Enzymatic and transcriptional regulation of the cytoplasmic acetyl-CoA hydrolase ACOT12 publication-title: J. Lipid Res. contributor: fullname: Sugimoto – volume: 50 start-page: 2139 year: 2009 end-page: 2147 ident: bib69 article-title: Bile acids: the role of peroxisomes publication-title: J. Lipid Res. contributor: fullname: Wanders – volume: 222 start-page: 803 year: 1994 end-page: 811 ident: bib14 article-title: Characterization of acyl-CoA thioesterase activity in isolated rat liver peroxisomes publication-title: Eur. J. Biochem. contributor: fullname: Alexson – volume: 278 start-page: 34237 year: 2003 end-page: 34344 ident: bib70 article-title: The human bile acid-CoA:amino acid publication-title: J. Biol. Chem. contributor: fullname: Alexson – volume: 41 start-page: 99 year: 2002 end-page: 130 ident: bib9 article-title: The role acyl-CoA thioesterases play in mediating intracellular lipid metabolism publication-title: Prog. Lipid Res. contributor: fullname: Alexson – volume: 32 start-page: 1 year: 2000 end-page: 8 ident: bib51 article-title: In silico search for genes encoding peroxisomal proteins in publication-title: Cell Biochem. Biophys. contributor: fullname: Tabak – volume: 1822 start-page: 1397 year: 2012 end-page: 1410 ident: bib11 article-title: The emerging role of acyl-CoA thioesterases and acyltransferases in regulating peroxisomal lipid metabolism publication-title: Biochim. Biophys. Acta contributor: fullname: Alexson – volume: 40 start-page: 601 year: 1999 end-page: 609 ident: bib37 article-title: Stereochemistry of the alpha-oxidation of 3-methyl-branched fatty acids in rat liver publication-title: J. Lipid Res. contributor: fullname: van Veldhoven – volume: 142 start-page: 177 year: 1984 end-page: 181 ident: bib63 article-title: A cold-labile acetyl-coenzyme-A hydrolase from the supernatant fraction of rat liver. Reactivation and reconstitution of the active species from the inactive monomer publication-title: Eur. J. Biochem. contributor: fullname: Sakamoto – volume: 110 start-page: 1279 year: 2013 end-page: 1284 ident: bib13 article-title: Intrinsic acyl-CoA thioesterase activity of a peroxisomal ATP binding cassette transporter is required for transport and metabolism of fatty acids publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Theodoulou – volume: 290 start-page: 629 year: 2002 end-page: 634 ident: bib40 article-title: Demonstration of dimethylnonanoyl-CoA thioesterase activity in rat liver peroxisomes followed by purification and molecular cloning of the thioesterase involved publication-title: Biochem. Biophys. Res. Commun. contributor: fullname: Wanders – volume: 28 start-page: 946 year: 2000 end-page: 947 ident: bib46 article-title: Two families of acyl-CoA thioesterases in Arabidopsis publication-title: Biochem. Soc. Trans. contributor: fullname: Browse – volume: 297 start-page: 127 year: 2004 end-page: 141 ident: bib52 article-title: Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis publication-title: Exp. Cell Res. contributor: fullname: Saito – volume: 279 start-page: 19574 year: 2004 end-page: 19579 ident: bib20 article-title: Peroxisomal fatty acid oxidation is a substantial source of the acetyl moiety of malonyl-CoA in rat heart publication-title: J. Biol. Chem. contributor: fullname: Des Rosiers – volume: 63 start-page: 1752 year: 2006 end-page: 1765 ident: bib31 article-title: Phytanic acid: production from phytol, its breakdown and role in human disease publication-title: Cell. Mol. Life Sci. contributor: fullname: Wanders – volume: 274 start-page: 34317 year: 1999 end-page: 34326 ident: bib16 article-title: Peroxisome proliferator-induced long chain acyl-CoA thioesterases comprise a highly conserved novel multi-gene family involved in lipid metabolism publication-title: J. Biol. Chem. contributor: fullname: Alexson – volume: 1822 start-page: 1374 year: 2012 end-page: 1389 ident: bib83 article-title: Transfer of metabolites across the peroxisomal membrane publication-title: Biochim. Biophys. Acta contributor: fullname: Hiltunen – volume: 6 start-page: 2045 year: 2007 end-page: 2057 ident: bib58 article-title: Proteomic characterization of mouse kidney peroxisomes by tandem mass spectrometry and protein correlation profiling publication-title: Mol. Cell. Proteomics contributor: fullname: Warscheid – volume: 269 start-page: 19375 year: 1994 end-page: 19379 ident: bib95 article-title: Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid-CoA:amino acid publication-title: J. Biol. Chem. contributor: fullname: Diasio – volume: 43 start-page: 14332 year: 2004 end-page: 14339 ident: bib73 article-title: Assignment of endogenous substrates to enzymes by global metabolite profiling publication-title: Biochemistry contributor: fullname: Cravatt – volume: 22 start-page: 584 year: 1983 end-page: 590 ident: bib62 article-title: Effects of nucleotides on a cold labile acetyl-CoA hydrolase from the supernatant fraction of rat liver publication-title: Biochemistry contributor: fullname: Sakamoto – volume: 75 start-page: 295 year: 2006 end-page: 332 ident: bib4 article-title: Biochemistry of mammalian peroxisomes revisited publication-title: Annu. Rev. Biochem. contributor: fullname: Waterham – volume: 280 start-page: 38125 year: 2005 end-page: 38132 ident: bib24 article-title: The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes publication-title: J. Biol. Chem. contributor: fullname: Alexson – volume: 35 start-page: 865 year: 2007 end-page: 869 ident: bib3 article-title: Peroxisomes, Refsum's disease and the alpha- and omega-oxidation of phytanic acid publication-title: Biochem. Soc. Trans. contributor: fullname: Komen – volume: 222 start-page: 313 year: 1994 end-page: 323 ident: bib38 article-title: Purification and properties of an alpha-methylacyl-CoA racemase from rat liver publication-title: Eur. J. Biochem. contributor: fullname: Conzelmann – volume: 226 start-page: 78 year: 2001 end-page: 84 ident: bib94 article-title: Physiological role of UCP3 may be export of fatty acids from mitochondria when fatty acid oxidation predominates: an hypothesis publication-title: Proc. Soc. Exp. Biol. Med. contributor: fullname: Harper – volume: 9 start-page: 113 year: 2010 end-page: 124 ident: bib59 article-title: Peroxisomes from the heavy mitochondrial fraction: isolation by zonal free flow electrophoresis and quantitative mass spectrometrical characterization publication-title: J. Proteome Res. contributor: fullname: Völkl – volume: 430 start-page: 54 year: 2013 end-page: 59 ident: bib80 article-title: -Acyl taurines trigger insulin secretion by increasing calcium flux in pancreatic β-cells publication-title: Biochem. Biophys. Res. Commun. contributor: fullname: Hunt – volume: 280 start-page: 9265 year: 2005 end-page: 9271 ident: bib21 article-title: Peroxisomal and mitochondrial oxidation of fatty acids in the heart, assessed from the 13C labeling of malonyl-CoA and the acetyl moiety of citrate publication-title: J. Biol. Chem. contributor: fullname: Brunengraber – volume: 222 start-page: 795 year: 1994 end-page: 801 ident: bib35 article-title: Large-scale purification and further characterization of rat pristanoyl-CoA oxidase publication-title: Eur. J. Biochem. contributor: fullname: Mannaerts – volume: 357 start-page: 33 year: 2001 end-page: 38 ident: bib88 article-title: The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives publication-title: Biochem. J. contributor: fullname: McLennan – volume: 259 start-page: 13089 year: 1984 end-page: 13095 ident: bib28 article-title: Properties of purified carnitine acyltransferases of mouse liver peroxisomes publication-title: J. Biol. Chem. contributor: fullname: Bieber – volume: 77 start-page: 1759 year: 2005 end-page: 1766 ident: bib72 article-title: Discovery metabolite profiling – forging functional connections between the proteome and metabolome publication-title: Life Sci. contributor: fullname: Cravatt – volume: 877 start-page: 2890 year: 2009 end-page: 2894 ident: bib75 article-title: Targeted lipidomics approach for endogenous publication-title: J. Chromatogr. B Anal. Technol. Biomed. Life Sci. contributor: fullname: Walker – volume: 144 start-page: 655 year: 2008 end-page: 663 ident: bib90 article-title: The nudix hydrolase 7 is an acyl-CoA diphosphatase involved in regulating peroxisomal coenzyme A homeostasis publication-title: J. Biochem. contributor: fullname: Hunt – volume: 270 start-page: 4908 year: 1995 end-page: 4915 ident: bib18 article-title: Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells publication-title: J. Biol. Chem. contributor: fullname: Reddy – volume: 65 start-page: 982 year: 2008 end-page: 990 ident: bib29 article-title: Short- and medium-chain carnitine acyltransferases and acyl-CoA thioesterases in mouse provide complementary systems for transport of beta-oxidation products out of peroxisomes publication-title: Cell. Mol. Life Sci. contributor: fullname: Alexson – volume: 255 start-page: 5215 year: 1980 end-page: 5223 ident: bib57 article-title: Purification and characterization of an extramitochondrial acetyl coenzyme A hydrolase from rat liver publication-title: J. Biol. Chem. contributor: fullname: Utter – volume: 389 start-page: 397 year: 2005 end-page: 401 ident: bib22 article-title: Probing peroxisomal beta-oxidation and the labelling of acetyl-CoA proxies with [1-(13C)]octanoate and [3-(13C)]octanoate in the perfused rat liver publication-title: Biochem. J. contributor: fullname: Brunengraber – volume: 52 start-page: 337 year: 2011 end-page: 344 ident: bib76 article-title: An anatomical and temporal portrait of physiological substrates for fatty acid amide hydrolase publication-title: J. Lipid Res. contributor: fullname: Cravatt – volume: 263 start-page: 213 year: 1999 end-page: 218 ident: bib41 article-title: Molecular cloning and expression of human carnitine octanoyltransferase: evidence for its role in the peroxisomal β-oxidation of branched-chain fatty acids publication-title: Biochem. Biophys. Res. Commun. contributor: fullname: Wanders – volume: 374 start-page: 329 year: 2003 end-page: 335 ident: bib89 article-title: Mammalian NADH diphosphatases of the Nudix family: cloning and characterization of the human peroxisomal NUDT12 protein publication-title: Biochem. J. contributor: fullname: McLennan – volume: 64 start-page: 3271 year: 2007 end-page: 3281 ident: bib33 article-title: Phytanic acid impairs mitochondrial respiration through protonophoric action publication-title: Cell. Mol. Life Sci. contributor: fullname: Willems – volume: 357 start-page: 335 year: 2007 end-page: 340 ident: bib91 article-title: Demonstration of bile acid transport across the mammalian peroxisomal membrane publication-title: Biochem. Biophys. Res. Commun. contributor: fullname: Wanders – volume: 299 start-page: 494 year: 2002 end-page: 497 ident: bib85 article-title: Identification of human PMP34 as a peroxisomal ATP transporter publication-title: Biochem. Biophys. Res. Commun. contributor: fullname: Wanders – volume: 281 start-page: 11729 year: 2006 end-page: 11735 ident: bib55 article-title: The peroxisomal acyl-CoA thioesterase Pte1p from publication-title: J. Biol. Chem. contributor: fullname: Poirier – volume: 75 start-page: 1262 year: 2009 end-page: 1279 ident: bib79 article-title: Pharmacology of vanilloid transient receptor potential cation channels publication-title: Mol. Pharmacol. contributor: fullname: Nilius – volume: 93 start-page: 13748 year: 1996 end-page: 13753 ident: bib36 article-title: Molecular characterization of the human peroxisomal branched-chain acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and evidence for the absence of the protein in Zellweger syndrome publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Van Veldhoven – volume: 110 start-page: 392 year: 2010 end-page: 396 ident: bib45 article-title: Genetic replacement of tesB with PTE1 affects chain-length proportions of 3-hydroxyalkanoic acids produced through β-oxidation of oleic acid in publication-title: J. Biosci. Bioeng. contributor: fullname: Maeda – volume: 274 start-page: 9216 year: 1999 end-page: 9223 ident: bib48 article-title: Identification of peroxisomal acyl-CoA thioesterases in yeast and human publication-title: J. Biol. Chem. contributor: fullname: Gould – volume: 1831 start-page: 1467 year: 2013 end-page: 1474 ident: bib56 article-title: Peroxisomes contribute to the acylcarnitine production when the carnitine shuttle is deficient publication-title: Biochim. Biophys. Acta contributor: fullname: Houten – volume: 19 start-page: 1281 year: 2010 end-page: 1295 ident: bib7 article-title: Thioesterases: a new perspective based on their primary and tertiary structures publication-title: Protein Sci. contributor: fullname: Reilly – volume: 87 start-page: 1735 year: 1980 end-page: 1746 ident: bib17 article-title: Purification and properties of acyl-CoA oxidase from rat liver publication-title: J. Biochem. contributor: fullname: Ui – volume: 47 start-page: 3917 year: 2008 end-page: 3925 ident: bib78 article-title: Oxidative metabolism of a fatty acid amide hydrolase-regulated lipid, arachidonyltaurine publication-title: Biochemistry contributor: fullname: Marnett – volume: 262 start-page: 41 year: 1989 end-page: 46 ident: bib15 article-title: The presence of acyl-CoA hydrolase in rat brown-adipose-tissue peroxisomes publication-title: Biochem. J. contributor: fullname: Berge – volume: 115 start-page: 328 year: 1994 end-page: 332 ident: bib61 article-title: Subcellular distribution of ATP-stimulated and ADP-inhibited acetyl-CoA hydrolase in livers from control and clofibrate-treated rats: comparison of the cytosolic and peroxisomal enzyme publication-title: J. Biochem. (Tokyo) contributor: fullname: Isohashi – volume: 164 start-page: 1753 year: 2011 end-page: 1766 ident: bib86 article-title: Mammalian peroxisomal ABC transporters: from endogenous substrates to pathology and clinical significance publication-title: Br. J. Pharmacol. contributor: fullname: Wanders – volume: 12 start-page: 625 year: 1980 end-page: 630 ident: bib19 article-title: Fatty acid products of peroxisomal beta-oxidation publication-title: Int. J. Biochem. contributor: fullname: Borrebaek – volume: 5 start-page: 1 year: 2004 end-page: 14 ident: bib6 article-title: The Hotdog fold: wrapping up a superfamily of thioesterases and dehydratases publication-title: BMC Bioinf. contributor: fullname: Bateman – volume: 1811 start-page: 498 year: 2011 end-page: 507 ident: bib30 article-title: Phytanic acid metabolism in health and disease publication-title: Biochim. Biophys. Acta contributor: fullname: Ferdinandusse – volume: 238 start-page: 234 year: 1997 end-page: 239 ident: bib49 article-title: A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef publication-title: Biochem. Biophys. Res. Commun. contributor: fullname: Saito – volume: 393 start-page: 537 year: 2006 end-page: 543 ident: bib87 article-title: Proteomic analysis of mouse kidney peroxisomes: identification of RP2p as a peroxisomal nudix hydrolase with acyl-CoA diphosphatase activity publication-title: Biochem. J. contributor: fullname: Wanders – volume: 10 start-page: 2863 year: 2010 end-page: 2895 ident: bib32 article-title: Biochemistry and genetics of inherited disorders of peroxisomal fatty acid metabolism publication-title: J. Lipid Res. contributor: fullname: Van Veldhoven – volume: 150 start-page: 489 year: 2000 end-page: 498 ident: bib26 article-title: Pex11p plays a primary role in medium-chain fatty acid oxidation, a process that affects peroxisome number and size in publication-title: J. Cell Biol. contributor: fullname: Hettema – volume: 6 start-page: e19521 year: 2011 ident: bib64 article-title: Comparative structural analysis of lipid binding START domains publication-title: PLoS One contributor: fullname: Lehtió – volume: 209 start-page: 276 year: 2013 end-page: 283 ident: bib53 article-title: Acyl-CoA thioesterase 8 is a specific protein related to nodal metastasis and prognosis of lung adenocarcinoma publication-title: Pathol. Res. Pract. contributor: fullname: Kim – volume: 108 start-page: 4794 year: 2011 end-page: 4799 ident: bib93 article-title: Proline- and acidic amino acid-rich basic leucine zipper proteins modulate peroxisome proliferator-activated receptor alpha (PPARalpha) activity publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Schibler – volume: 49 start-page: 366 year: 2010 end-page: 377 ident: bib8 article-title: Functional and structural properties of mammalian acyl-coenzyme A thioesterases publication-title: Prog. Lipid Res. contributor: fullname: Forwood – volume: 4 start-page: 411 year: 2010 end-page: 420 ident: bib12 article-title: Evolutionary divergence and functions of the human acyl-CoA thioesterase gene (ACOT ) family publication-title: Hum. Genomics contributor: fullname: Vasiliou – volume: 264 start-page: 10347 year: 1989 end-page: 10350 ident: bib65 article-title: Free acetate production by rat hepatocytes during peroxisomal fatty acid and dicarboxylic acid oxidation publication-title: J. Biol. Chem. contributor: fullname: Bremer – volume: 21 start-page: 99 year: 2007 end-page: 107 ident: bib66 article-title: A peroxisomal acyltransferase in mouse identifies a novel pathway for taurine conjugation of fatty acids publication-title: FASEB J. contributor: fullname: Hunt – volume: 443 start-page: 241 year: 2012 end-page: 247 ident: bib84 article-title: The human gene SLC25A17 encodes a peroxisomal transporter of coenzyme A, FAD and NAD publication-title: Biochem. J. contributor: fullname: Palmieri – volume: 20 start-page: 1855 year: 2006 end-page: 1864 ident: bib25 article-title: Analysis of mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent functional evolution results in a reduced number of peroxisomal ACOTs publication-title: FASEB J. contributor: fullname: Alexson – volume: 81 start-page: 191 year: 2009 end-page: 205 ident: bib67 article-title: Novel endogenous N-acyl glycines: identification and characterization publication-title: Vitam. Horm. contributor: fullname: Walker – volume: 279 start-page: 7487 year: 2004 end-page: 7494 ident: bib47 article-title: Biochemical and molecular characterization of ACH2, an acyl-CoA thioesterase from publication-title: J. Biol. Chem. contributor: fullname: Browse – volume: 74 start-page: 411 year: 2005 end-page: 432 ident: bib77 article-title: Structure and function of fatty acid amide hydrolase publication-title: Annu. Rev. Biochem. contributor: fullname: Cravatt – volume: 44 start-page: 2242 year: 2003 end-page: 2249 ident: bib96 article-title: Rat liver bile acid CoA:amino acid publication-title: J. Lipid Res. contributor: fullname: Falany – volume: 279 start-page: 21841 year: 2004 end-page: 21848 ident: bib23 article-title: Molecular cloning and characterization of two mouse peroxisome proliferator-activated receptor alpha (PPARα)-regulated peroxisomal acyl-CoA thioesterases publication-title: J. Biol. Chem. contributor: fullname: Hunt – volume: 13 start-page: 1378 year: 2012 end-page: 1392 ident: bib43 article-title: An inventory of peroxisomal proteins and pathways in publication-title: Traffic contributor: fullname: McNew – volume: 45 start-page: 9007 year: 2006 end-page: 9015 ident: bib74 article-title: A FAAH-regulated class of publication-title: Biochemistry contributor: fullname: Cravatt – volume: 44 start-page: 2242 year: 2003 ident: 10.1016/j.biochi.2013.12.018_bib96 article-title: Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization publication-title: J. Lipid Res. doi: 10.1194/jlr.M300128-JLR200 contributor: fullname: He – volume: 110 start-page: 1279 year: 2013 ident: 10.1016/j.biochi.2013.12.018_bib13 article-title: Intrinsic acyl-CoA thioesterase activity of a peroxisomal ATP binding cassette transporter is required for transport and metabolism of fatty acids publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1218034110 contributor: fullname: De Marcos – volume: 430 start-page: 54 year: 2013 ident: 10.1016/j.biochi.2013.12.018_bib80 article-title: N-Acyl taurines trigger insulin secretion by increasing calcium flux in pancreatic β-cells publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2012.11.026 contributor: fullname: Waluk – volume: 247 start-page: 3123 year: 1972 ident: 10.1016/j.biochi.2013.12.018_bib44 article-title: Purification and properties of fatty acyl thioesterase I from Escherichia coli publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)45222-8 contributor: fullname: Bonner – volume: 269 start-page: 19375 year: 1994 ident: 10.1016/j.biochi.2013.12.018_bib95 article-title: Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid-CoA:amino acid N-acyltransferase publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)32178-6 contributor: fullname: Falany – volume: 19 start-page: 1281 year: 2010 ident: 10.1016/j.biochi.2013.12.018_bib7 article-title: Thioesterases: a new perspective based on their primary and tertiary structures publication-title: Protein Sci. doi: 10.1002/pro.417 contributor: fullname: Cantu – volume: 110 start-page: 392 year: 2010 ident: 10.1016/j.biochi.2013.12.018_bib45 article-title: Genetic replacement of tesB with PTE1 affects chain-length proportions of 3-hydroxyalkanoic acids produced through β-oxidation of oleic acid in Escherichia coli publication-title: J. Biosci. Bioeng. doi: 10.1016/j.jbiosc.2010.05.004 contributor: fullname: Seto – volume: 21 start-page: 99 year: 2007 ident: 10.1016/j.biochi.2013.12.018_bib66 article-title: A peroxisomal acyltransferase in mouse identifies a novel pathway for taurine conjugation of fatty acids publication-title: FASEB J. doi: 10.1096/fj.06-6919com contributor: fullname: Reilly – volume: 259 start-page: 13089 year: 1984 ident: 10.1016/j.biochi.2013.12.018_bib28 article-title: Properties of purified carnitine acyltransferases of mouse liver peroxisomes publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)90661-7 contributor: fullname: Farrell – volume: 279 start-page: 21841 year: 2004 ident: 10.1016/j.biochi.2013.12.018_bib23 article-title: Molecular cloning and characterization of two mouse peroxisome proliferator-activated receptor alpha (PPARα)-regulated peroxisomal acyl-CoA thioesterases publication-title: J. Biol. Chem. doi: 10.1074/jbc.M313863200 contributor: fullname: Westin – volume: 13 start-page: 1378 year: 2012 ident: 10.1016/j.biochi.2013.12.018_bib43 article-title: An inventory of peroxisomal proteins and pathways in Drosophila melanogaster publication-title: Traffic doi: 10.1111/j.1600-0854.2012.01393.x contributor: fullname: Faust – volume: 115 start-page: 328 year: 1994 ident: 10.1016/j.biochi.2013.12.018_bib61 article-title: Subcellular distribution of ATP-stimulated and ADP-inhibited acetyl-CoA hydrolase in livers from control and clofibrate-treated rats: comparison of the cytosolic and peroxisomal enzyme publication-title: J. Biochem. (Tokyo) doi: 10.1093/oxfordjournals.jbchem.a124337 contributor: fullname: Nakanishi – volume: 278 start-page: 34237 year: 2003 ident: 10.1016/j.biochi.2013.12.018_bib70 article-title: The human bile acid-CoA:amino acid N-acyltransferase functions in conjugation of fatty acids to glycine publication-title: J. Biol. Chem. doi: 10.1074/jbc.M300987200 contributor: fullname: O'Byrne – volume: 269 start-page: 11025 year: 1994 ident: 10.1016/j.biochi.2013.12.018_bib71 article-title: Nonhomogeneous labeling of liver extra-mitochondrial acetyl-CoA. Implications for the probing of lipogenic acetyl-CoA via drug acetylation and for the production of acetate by the liver publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)78086-7 contributor: fullname: Zhang – volume: 142 start-page: 177 year: 1984 ident: 10.1016/j.biochi.2013.12.018_bib63 article-title: A cold-labile acetyl-coenzyme-A hydrolase from the supernatant fraction of rat liver. Reactivation and reconstitution of the active species from the inactive monomer publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1984.tb08267.x contributor: fullname: Isohashi – volume: 63 start-page: 1752 year: 2006 ident: 10.1016/j.biochi.2013.12.018_bib31 article-title: Phytanic acid: production from phytol, its breakdown and role in human disease publication-title: Cell. Mol. Life Sci. doi: 10.1007/s00018-005-5463-y contributor: fullname: van den Brink – volume: 41 start-page: 99 year: 2002 ident: 10.1016/j.biochi.2013.12.018_bib9 article-title: The role acyl-CoA thioesterases play in mediating intracellular lipid metabolism publication-title: Prog. Lipid Res. doi: 10.1016/S0163-7827(01)00017-0 contributor: fullname: Hunt – volume: 255 start-page: 5215 year: 1980 ident: 10.1016/j.biochi.2013.12.018_bib57 article-title: Purification and characterization of an extramitochondrial acetyl coenzyme A hydrolase from rat liver publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)70773-X contributor: fullname: Prass – volume: 279 start-page: 19574 year: 2004 ident: 10.1016/j.biochi.2013.12.018_bib20 article-title: Peroxisomal fatty acid oxidation is a substantial source of the acetyl moiety of malonyl-CoA in rat heart publication-title: J. Biol. Chem. doi: 10.1074/jbc.M400162200 contributor: fullname: Reszko – volume: 74 start-page: 411 year: 2005 ident: 10.1016/j.biochi.2013.12.018_bib77 article-title: Structure and function of fatty acid amide hydrolase publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.74.082803.133450 contributor: fullname: McKinney – volume: 33 start-page: 88 year: 2011 ident: 10.1016/j.biochi.2013.12.018_bib2 publication-title: BioEssays doi: 10.1002/bies.201000097 contributor: fullname: Speijer – year: 2013 ident: 10.1016/j.biochi.2013.12.018_bib1 article-title: A metabolic scenario for the evolutionary origin of peroxisomes from the endomembranous system publication-title: Cell. Mol. Life Sci. contributor: fullname: Gabaldón – volume: 222 start-page: 313 year: 1994 ident: 10.1016/j.biochi.2013.12.018_bib38 article-title: Purification and properties of an alpha-methylacyl-CoA racemase from rat liver publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1994.tb18870.x contributor: fullname: Schmitz – volume: 297 start-page: 127 year: 2004 ident: 10.1016/j.biochi.2013.12.018_bib52 article-title: Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis publication-title: Exp. Cell Res. doi: 10.1016/j.yexcr.2004.02.029 contributor: fullname: Ishizuka – volume: 279 start-page: 7487 year: 2004 ident: 10.1016/j.biochi.2013.12.018_bib47 article-title: Biochemical and molecular characterization of ACH2, an acyl-CoA thioesterase from Arabidopsis thaliana publication-title: J. Biol. Chem. doi: 10.1074/jbc.M309532200 contributor: fullname: Tilton – volume: 9 start-page: 113 year: 2010 ident: 10.1016/j.biochi.2013.12.018_bib59 article-title: Peroxisomes from the heavy mitochondrial fraction: isolation by zonal free flow electrophoresis and quantitative mass spectrometrical characterization publication-title: J. Proteome Res. doi: 10.1021/pr9004663 contributor: fullname: Islinger – volume: 4 start-page: 411 year: 2010 ident: 10.1016/j.biochi.2013.12.018_bib12 article-title: Evolutionary divergence and functions of the human acyl-CoA thioesterase gene (ACOT ) family publication-title: Hum. Genomics doi: 10.1186/1479-7364-4-6-411 contributor: fullname: Brocker – volume: 263 start-page: 213 year: 1999 ident: 10.1016/j.biochi.2013.12.018_bib41 article-title: Molecular cloning and expression of human carnitine octanoyltransferase: evidence for its role in the peroxisomal β-oxidation of branched-chain fatty acids publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.1999.1340 contributor: fullname: Ferdinandusse – volume: 20 start-page: 1855 year: 2006 ident: 10.1016/j.biochi.2013.12.018_bib25 article-title: Analysis of mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent functional evolution results in a reduced number of peroxisomal ACOTs publication-title: FASEB J. doi: 10.1096/fj.06-6042com contributor: fullname: Hunt – volume: 1822 start-page: 1374 year: 2012 ident: 10.1016/j.biochi.2013.12.018_bib83 article-title: Transfer of metabolites across the peroxisomal membrane publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbadis.2011.12.011 contributor: fullname: Antonenkov – volume: 23 start-page: 424 year: 1988 ident: 10.1016/j.biochi.2013.12.018_bib42 article-title: Disposition and metabolism of pristane in rat publication-title: Lipids doi: 10.1007/BF02535514 contributor: fullname: Le Bon – volume: 1831 start-page: 1467 year: 2013 ident: 10.1016/j.biochi.2013.12.018_bib56 article-title: Peroxisomes contribute to the acylcarnitine production when the carnitine shuttle is deficient publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbalip.2013.06.007 contributor: fullname: Violante – volume: 281 start-page: 11729 year: 2006 ident: 10.1016/j.biochi.2013.12.018_bib55 article-title: The peroxisomal acyl-CoA thioesterase Pte1p from Saccharomyces cerevisiae is required for efficient degradation of short straight chain and branched chain fatty acids publication-title: J. Biol. Chem. doi: 10.1074/jbc.M511762200 contributor: fullname: Maeda – volume: 226 start-page: 78 year: 2001 ident: 10.1016/j.biochi.2013.12.018_bib94 article-title: Physiological role of UCP3 may be export of fatty acids from mitochondria when fatty acid oxidation predominates: an hypothesis publication-title: Proc. Soc. Exp. Biol. Med. doi: 10.1177/153537020122600204 contributor: fullname: Himms-Hagen – volume: 257 start-page: 615 year: 1999 ident: 10.1016/j.biochi.2013.12.018_bib27 article-title: Human very-long-chain acyl-CoA synthetase: cloning, topography and relevance to branched-chain fatty acid metabolism publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.1999.0510 contributor: fullname: Steinberg – volume: 150 start-page: 489 year: 2000 ident: 10.1016/j.biochi.2013.12.018_bib26 article-title: Pex11p plays a primary role in medium-chain fatty acid oxidation, a process that affects peroxisome number and size in Saccharomyces cerevisiae publication-title: J. Cell Biol. doi: 10.1083/jcb.150.3.489 contributor: fullname: van Roermund – volume: 47 start-page: 355 year: 2012 ident: 10.1016/j.biochi.2013.12.018_bib82 article-title: N-Acyl taurines are anti-proliferative in prostate cancer cells publication-title: Lipids doi: 10.1007/s11745-011-3639-9 contributor: fullname: Chatzakos – volume: 262 start-page: 41 year: 1989 ident: 10.1016/j.biochi.2013.12.018_bib15 article-title: The presence of acyl-CoA hydrolase in rat brown-adipose-tissue peroxisomes publication-title: Biochem. J. doi: 10.1042/bj2620041 contributor: fullname: Alexson – volume: 35 start-page: 865 year: 2007 ident: 10.1016/j.biochi.2013.12.018_bib3 article-title: Peroxisomes, Refsum's disease and the alpha- and omega-oxidation of phytanic acid publication-title: Biochem. Soc. Trans. doi: 10.1042/BST0350865 contributor: fullname: Wanders – volume: 222 start-page: 795 year: 1994 ident: 10.1016/j.biochi.2013.12.018_bib35 article-title: Large-scale purification and further characterization of rat pristanoyl-CoA oxidase publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1994.tb18926.x contributor: fullname: van Veldhoven – volume: 52 start-page: 337 year: 2011 ident: 10.1016/j.biochi.2013.12.018_bib76 article-title: An anatomical and temporal portrait of physiological substrates for fatty acid amide hydrolase publication-title: J. Lipid Res. doi: 10.1194/jlr.M012153 contributor: fullname: Long – volume: 77 start-page: 1759 year: 2005 ident: 10.1016/j.biochi.2013.12.018_bib72 article-title: Discovery metabolite profiling – forging functional connections between the proteome and metabolome publication-title: Life Sci. doi: 10.1016/j.lfs.2005.05.019 contributor: fullname: Saghatelian – volume: 49 start-page: 366 year: 2010 ident: 10.1016/j.biochi.2013.12.018_bib8 article-title: Functional and structural properties of mammalian acyl-coenzyme A thioesterases publication-title: Prog. Lipid Res. doi: 10.1016/j.plipres.2010.04.001 contributor: fullname: Kirkby – volume: 47 start-page: 3917 year: 2008 ident: 10.1016/j.biochi.2013.12.018_bib78 article-title: Oxidative metabolism of a fatty acid amide hydrolase-regulated lipid, arachidonyltaurine publication-title: Biochemistry doi: 10.1021/bi702530z contributor: fullname: Turman – volume: 3 start-page: 159 year: 2007 ident: 10.1016/j.biochi.2013.12.018_bib92 article-title: Amino acid conjugation: contribution to the metabolism and toxicity of xenobiotic carboxylic acids publication-title: Expert Opin. Drug Metab. Toxicol. doi: 10.1517/17425255.3.2.159 contributor: fullname: Knights – volume: 45 start-page: 9007 year: 2006 ident: 10.1016/j.biochi.2013.12.018_bib74 article-title: A FAAH-regulated class of N-acyl taurines that activates TRP ion channels publication-title: Biochemistry doi: 10.1021/bi0608008 contributor: fullname: Saghatelian – volume: 277 start-page: 1128 year: 2002 ident: 10.1016/j.biochi.2013.12.018_bib39 article-title: Characterization of an acyl-CoA thioesterase that functions as a major regulator of peroxisomal lipid metabolism publication-title: J. Biol. Chem. doi: 10.1074/jbc.M106458200 contributor: fullname: Hunt – volume: 290 start-page: 629 year: 2002 ident: 10.1016/j.biochi.2013.12.018_bib40 article-title: Demonstration of dimethylnonanoyl-CoA thioesterase activity in rat liver peroxisomes followed by purification and molecular cloning of the thioesterase involved publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.2001.6245 contributor: fullname: Ofman – volume: 5 start-page: 1 year: 2004 ident: 10.1016/j.biochi.2013.12.018_bib6 article-title: The Hotdog fold: wrapping up a superfamily of thioesterases and dehydratases publication-title: BMC Bioinf. doi: 10.1186/1471-2105-5-109 contributor: fullname: Dillon – volume: 274 start-page: 9216 year: 1999 ident: 10.1016/j.biochi.2013.12.018_bib48 article-title: Identification of peroxisomal acyl-CoA thioesterases in yeast and human publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.14.9216 contributor: fullname: Jones – volume: 139 start-page: 1195 year: 1986 ident: 10.1016/j.biochi.2013.12.018_bib50 article-title: Coenzyme A in purified peroxisomes is not freely soluble in the matrix but firmly bound to a matrix protein publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/S0006-291X(86)80304-7 contributor: fullname: Van Veldhoven – volume: 209 start-page: 276 year: 2013 ident: 10.1016/j.biochi.2013.12.018_bib53 article-title: Acyl-CoA thioesterase 8 is a specific protein related to nodal metastasis and prognosis of lung adenocarcinoma publication-title: Pathol. Res. Pract. doi: 10.1016/j.prp.2013.02.008 contributor: fullname: Jung – volume: 374 start-page: 329 year: 2003 ident: 10.1016/j.biochi.2013.12.018_bib89 article-title: Mammalian NADH diphosphatases of the Nudix family: cloning and characterization of the human peroxisomal NUDT12 protein publication-title: Biochem. J. doi: 10.1042/bj20030441 contributor: fullname: AbdelRaheim – volume: 12 start-page: 625 year: 1980 ident: 10.1016/j.biochi.2013.12.018_bib19 article-title: Fatty acid products of peroxisomal beta-oxidation publication-title: Int. J. Biochem. doi: 10.1016/0020-711X(80)90015-4 contributor: fullname: Osmundsen – volume: 393 start-page: 537 year: 2006 ident: 10.1016/j.biochi.2013.12.018_bib87 article-title: Proteomic analysis of mouse kidney peroxisomes: identification of RP2p as a peroxisomal nudix hydrolase with acyl-CoA diphosphatase activity publication-title: Biochem. J. doi: 10.1042/BJ20050893 contributor: fullname: Ofman – volume: 389 start-page: 397 year: 2005 ident: 10.1016/j.biochi.2013.12.018_bib22 article-title: Probing peroxisomal beta-oxidation and the labelling of acetyl-CoA proxies with [1-(13C)]octanoate and [3-(13C)]octanoate in the perfused rat liver publication-title: Biochem. J. doi: 10.1042/BJ20050144 contributor: fullname: Kasumov – volume: 222 start-page: 803 year: 1994 ident: 10.1016/j.biochi.2013.12.018_bib14 article-title: Characterization of acyl-CoA thioesterase activity in isolated rat liver peroxisomes publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1994.tb18927.x contributor: fullname: Wilcke – volume: 50 start-page: 2139 year: 2009 ident: 10.1016/j.biochi.2013.12.018_bib69 article-title: Bile acids: the role of peroxisomes publication-title: J. Lipid Res. doi: 10.1194/jlr.R900009-JLR200 contributor: fullname: Ferdinandusse – volume: 282 start-page: 26707 year: 2007 ident: 10.1016/j.biochi.2013.12.018_bib34 article-title: Peroxisomes contain a specific phytanoyl-CoA/pristanoyl-CoA thioesterase acting as a novel auxiliary enzyme in alpha- and beta-oxidation of methyl-branched fatty acids in mouse publication-title: J. Biol. Chem. doi: 10.1074/jbc.M703718200 contributor: fullname: Westin – volume: 108 start-page: 4794 year: 2011 ident: 10.1016/j.biochi.2013.12.018_bib93 article-title: Proline- and acidic amino acid-rich basic leucine zipper proteins modulate peroxisome proliferator-activated receptor alpha (PPARalpha) activity publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1002862108 contributor: fullname: Gachon – volume: 6 start-page: 2045 year: 2007 ident: 10.1016/j.biochi.2013.12.018_bib58 article-title: Proteomic characterization of mouse kidney peroxisomes by tandem mass spectrometry and protein correlation profiling publication-title: Mol. Cell. Proteomics doi: 10.1074/mcp.M700169-MCP200 contributor: fullname: Wiese – volume: 443 start-page: 241 year: 2012 ident: 10.1016/j.biochi.2013.12.018_bib84 article-title: The human gene SLC25A17 encodes a peroxisomal transporter of coenzyme A, FAD and NAD+ publication-title: Biochem. J. doi: 10.1042/BJ20111420 contributor: fullname: Agrimi – volume: 75 start-page: 1262 year: 2009 ident: 10.1016/j.biochi.2013.12.018_bib79 article-title: Pharmacology of vanilloid transient receptor potential cation channels publication-title: Mol. Pharmacol. doi: 10.1124/mol.109.055624 contributor: fullname: Vriens – volume: 357 start-page: 33 year: 2001 ident: 10.1016/j.biochi.2013.12.018_bib88 article-title: The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives publication-title: Biochem. J. doi: 10.1042/0264-6021:3570033 contributor: fullname: Gasmi – volume: 47 start-page: 405 year: 2008 ident: 10.1016/j.biochi.2013.12.018_bib10 article-title: Novel functions of acyl-CoA thioesterases and acyltransferases as auxiliary enzymes in peroxisomal lipid metabolism publication-title: Prog. Lipid Res. doi: 10.1016/j.plipres.2008.05.001 contributor: fullname: Hunt – volume: 75 start-page: 295 year: 2006 ident: 10.1016/j.biochi.2013.12.018_bib4 article-title: Biochemistry of mammalian peroxisomes revisited publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.74.082803.133329 contributor: fullname: Wanders – volume: 280 start-page: 38125 year: 2005 ident: 10.1016/j.biochi.2013.12.018_bib24 article-title: The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes publication-title: J. Biol. Chem. doi: 10.1074/jbc.M508479200 contributor: fullname: Westin – volume: 6 start-page: e19521 year: 2011 ident: 10.1016/j.biochi.2013.12.018_bib64 article-title: Comparative structural analysis of lipid binding START domains publication-title: PLoS One doi: 10.1371/journal.pone.0019521 contributor: fullname: Thorsell – volume: 22 start-page: 584 year: 1983 ident: 10.1016/j.biochi.2013.12.018_bib62 article-title: Effects of nucleotides on a cold labile acetyl-CoA hydrolase from the supernatant fraction of rat liver publication-title: Biochemistry doi: 10.1021/bi00272a010 contributor: fullname: Isohashi – volume: 270 start-page: 4908 year: 1995 ident: 10.1016/j.biochi.2013.12.018_bib18 article-title: Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells publication-title: J. Biol. Chem. doi: 10.1074/jbc.270.9.4908 contributor: fullname: Chu – volume: 54 start-page: 2049 year: 2013 ident: 10.1016/j.biochi.2013.12.018_bib60 article-title: Enzymatic and transcriptional regulation of the cytoplasmic acetyl-CoA hydrolase ACOT12 publication-title: J. Lipid Res. doi: 10.1194/jlr.M030163 contributor: fullname: Horibata – volume: 83 start-page: 16 year: 2004 ident: 10.1016/j.biochi.2013.12.018_bib5 article-title: Peroxisomes, lipid metabolism, and peroxisomal disorders publication-title: Mol. Genet. Metab. doi: 10.1016/j.ymgme.2004.08.016 contributor: fullname: Wanders – volume: 87 start-page: 1735 year: 1980 ident: 10.1016/j.biochi.2013.12.018_bib17 article-title: Purification and properties of acyl-CoA oxidase from rat liver publication-title: J. Biochem. doi: 10.1093/oxfordjournals.jbchem.a132918 contributor: fullname: Osumi – volume: 1822 start-page: 1397 year: 2012 ident: 10.1016/j.biochi.2013.12.018_bib11 article-title: The emerging role of acyl-CoA thioesterases and acyltransferases in regulating peroxisomal lipid metabolism publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbadis.2012.03.009 contributor: fullname: Hunt – volume: 40 start-page: 601 year: 1999 ident: 10.1016/j.biochi.2013.12.018_bib37 article-title: Stereochemistry of the alpha-oxidation of 3-methyl-branched fatty acids in rat liver publication-title: J. Lipid Res. doi: 10.1016/S0022-2275(20)32139-8 contributor: fullname: Croes – volume: 10 start-page: 2863 year: 2010 ident: 10.1016/j.biochi.2013.12.018_bib32 article-title: Biochemistry and genetics of inherited disorders of peroxisomal fatty acid metabolism publication-title: J. Lipid Res. doi: 10.1194/jlr.R005959 contributor: fullname: Van Veldhoven – volume: 64 start-page: 3271 year: 2007 ident: 10.1016/j.biochi.2013.12.018_bib33 article-title: Phytanic acid impairs mitochondrial respiration through protonophoric action publication-title: Cell. Mol. Life Sci. doi: 10.1007/s00018-007-7357-7 contributor: fullname: Komen – volume: 32 start-page: 1 year: 2000 ident: 10.1016/j.biochi.2013.12.018_bib51 article-title: In silico search for genes encoding peroxisomal proteins in Saccharomyces cerevisiae publication-title: Cell Biochem. Biophys. doi: 10.1385/CBB:32:1-3:01 contributor: fullname: Kal – volume: 274 start-page: 34317 year: 1999 ident: 10.1016/j.biochi.2013.12.018_bib16 article-title: Peroxisome proliferator-induced long chain acyl-CoA thioesterases comprise a highly conserved novel multi-gene family involved in lipid metabolism publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.48.34317 contributor: fullname: Hunt – volume: 144 start-page: 655 year: 2008 ident: 10.1016/j.biochi.2013.12.018_bib90 article-title: The nudix hydrolase 7 is an acyl-CoA diphosphatase involved in regulating peroxisomal coenzyme A homeostasis publication-title: J. Biochem. doi: 10.1093/jb/mvn114 contributor: fullname: Reilly – volume: 93 start-page: 13748 year: 1996 ident: 10.1016/j.biochi.2013.12.018_bib36 article-title: Molecular characterization of the human peroxisomal branched-chain acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and evidence for the absence of the protein in Zellweger syndrome publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.93.24.13748 contributor: fullname: Baumgart – volume: 264 start-page: 10347 year: 1989 ident: 10.1016/j.biochi.2013.12.018_bib65 article-title: Free acetate production by rat hepatocytes during peroxisomal fatty acid and dicarboxylic acid oxidation publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)81625-8 contributor: fullname: Leighton – ident: 10.1016/j.biochi.2013.12.018_bib81 – volume: 1811 start-page: 498 year: 2011 ident: 10.1016/j.biochi.2013.12.018_bib30 article-title: Phytanic acid metabolism in health and disease publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbalip.2011.06.006 contributor: fullname: Wanders – volume: 43 start-page: 14332 year: 2004 ident: 10.1016/j.biochi.2013.12.018_bib73 article-title: Assignment of endogenous substrates to enzymes by global metabolite profiling publication-title: Biochemistry doi: 10.1021/bi0480335 contributor: fullname: Saghatelian – year: 2013 ident: 10.1016/j.biochi.2013.12.018_bib54 article-title: Molecular mechanisms of fatty acid synthase (FASN)-mediated resistance to anti-cancer treatments publication-title: Adv. Biol. Regul. contributor: fullname: Wu – volume: 299 start-page: 494 year: 2002 ident: 10.1016/j.biochi.2013.12.018_bib85 article-title: Identification of human PMP34 as a peroxisomal ATP transporter publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/S0006-291X(02)02663-3 contributor: fullname: Visser – volume: 877 start-page: 2890 year: 2009 ident: 10.1016/j.biochi.2013.12.018_bib75 article-title: Targeted lipidomics approach for endogenous N-acyl amino acids in rat brain tissue publication-title: J. Chromatogr. B Anal. Technol. Biomed. Life Sci. doi: 10.1016/j.jchromb.2009.01.002 contributor: fullname: Tan – volume: 65 start-page: 982 year: 2008 ident: 10.1016/j.biochi.2013.12.018_bib29 article-title: Short- and medium-chain carnitine acyltransferases and acyl-CoA thioesterases in mouse provide complementary systems for transport of beta-oxidation products out of peroxisomes publication-title: Cell. Mol. Life Sci. doi: 10.1007/s00018-008-7576-6 contributor: fullname: Westin – volume: 280 start-page: 9265 year: 2005 ident: 10.1016/j.biochi.2013.12.018_bib21 article-title: Peroxisomal and mitochondrial oxidation of fatty acids in the heart, assessed from the 13C labeling of malonyl-CoA and the acetyl moiety of citrate publication-title: J. Biol. Chem. doi: 10.1074/jbc.M412850200 contributor: fullname: Bian – volume: 144 start-page: 459 year: 2005 ident: 10.1016/j.biochi.2013.12.018_bib68 article-title: The expanding field of cannabimimetic and related lipid mediators publication-title: Br. J. Pharmacol. doi: 10.1038/sj.bjp.0706093 contributor: fullname: Bradshaw – volume: 81 start-page: 191 year: 2009 ident: 10.1016/j.biochi.2013.12.018_bib67 article-title: Novel endogenous N-acyl glycines: identification and characterization publication-title: Vitam. Horm. doi: 10.1016/S0083-6729(09)81008-X contributor: fullname: Bradshaw – volume: 164 start-page: 1753 year: 2011 ident: 10.1016/j.biochi.2013.12.018_bib86 article-title: Mammalian peroxisomal ABC transporters: from endogenous substrates to pathology and clinical significance publication-title: Br. J. Pharmacol. doi: 10.1111/j.1476-5381.2011.01435.x contributor: fullname: Kemp – volume: 28 start-page: 946 year: 2000 ident: 10.1016/j.biochi.2013.12.018_bib46 article-title: Two families of acyl-CoA thioesterases in Arabidopsis publication-title: Biochem. Soc. Trans. doi: 10.1042/bst0280946 contributor: fullname: Tilton – volume: 238 start-page: 234 year: 1997 ident: 10.1016/j.biochi.2013.12.018_bib49 article-title: A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.1997.7217 contributor: fullname: Watanabe – volume: 357 start-page: 335 year: 2007 ident: 10.1016/j.biochi.2013.12.018_bib91 article-title: Demonstration of bile acid transport across the mammalian peroxisomal membrane publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2007.03.083 contributor: fullname: Visser |
| SSID | ssj0005029 |
| Score | 2.4111118 |
| SecondaryResourceType | review_article |
| Snippet | Peroxisomes are nearly ubiquitous organelles involved in a number of metabolic pathways that vary between organisms and tissues. A common metabolic function in... |
| SourceID | swepub proquest crossref pubmed elsevier |
| SourceType | Open Access Repository Aggregation Database Index Database Publisher |
| StartPage | 45 |
| SubjectTerms | Acyl Coenzyme A - metabolism Acyl-CoA thioesterase Acyl-CoA:amino acid N-acyltransferase Acyltransferases - metabolism Animals Biological Transport - physiology Coenzyme A Coenzyme A - metabolism Coenzyme A-Transferases - metabolism Fatty Acids - metabolism Humans Lipid Metabolism Medicin och hälsovetenskap Nudix hydrolase Nudix Hydrolases Peroxisomal lipid metabolism Peroxisomes - metabolism Pyrophosphatases - metabolism Thiolester Hydrolases - metabolism β-Oxidation |
| Title | Regulation of peroxisomal lipid metabolism: The role of acyl-CoA and coenzyme A metabolizing enzymes |
| URI | https://dx.doi.org/10.1016/j.biochi.2013.12.018 https://www.ncbi.nlm.nih.gov/pubmed/24389458 https://search.proquest.com/docview/1508424483 http://kipublications.ki.se/Default.aspx?queryparsed=id:128329849 |
| Volume | 98 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnR3LjtMwcLSPA3BA0OVRHisjob2Zxo6TOtyiilUBsQdgpb1ZjuOIQJNUpCvRPfDtzORRXishccghzthxZibzsMczAM9FKPIgF5pHNoi48oXmqBQsd9pm0idFHnc1I9-dxctz9eYiutiDxXgWhsIqB9nfy_ROWg8tswGbs3VZzj4gewZJoEkKo5Onk304RHVEe7WH6eu3y7OfkR5BV6yM4Dl1GE_QdWFeWdm4TyXFeIXduiBV_7heQ_1tgf6RXrRTSad34PZgS7K0n-5d2PP1BI7SGv3oastOWBfd2S2bT-DGYqzsNoFbvyQhPIL8fV-OHgnEmoJR4vBvZdtUOPKqXJc5q_wGOWVVttVLhlzFKCCRIK3brviiSZmtc-YaX19tK8_SHfwVDs_61vYenJ---rhY8qH2AneRiDccseplolGSk49jVeRUmDlEtY69cEpbnTkZeLSXQqsC5aR0QmRUCUnGLkMf6D4c1E3tHwJzuY2sKkQ497EKCqGLRGQeDUvtUWDk8ynwEd9m3afYMGPs2WfT08cQfYyQBukzhflIFPMbqxjUAv_o-WykoUGU09aIrX1z2RrKik9H_nQ4hQc9cXdzkVQgXkXYW_bU3j2h1Nyk58zQ_qWky7Qe34eSMtEqmcLJNZ128AQbSRUl8aP__qrHcBPvVB8Y9wQONl8v_VO0lDbZMey_-C6Oh__hB6D8E6k |
| link.rule.ids | 230,314,780,784,885,4502,24116,27924,27925,45585,45679 |
| linkProvider | Elsevier |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwEB6VcigcEGx5LE8jod7MxomddbitVlQLtD1AK_VmOY6jBjbJimwltgd-OzN5rApUQuKQizN2nJnJzNj5PAPwRkQiCzKhubKB4tLnmqNTsNxpm4Y-ybO4rRl5fBIvzuTHc3W-A_PhLAzBKnvb39n01lr3LZOem5NVUUy-oHoGSaDJCuMiTye34LZUGP2iUr_9eQ3nEbSlyoiaE_lwfq4FeaVF7S4KQnhF7a4g1f642T_9HX_-kVy0dUiH9-FeH0myWTfZB7DjqxHszypcRZcbdsBabGe7aT6CvflQ120Ed6-lINyH7HNXjB7Fw-qcUdrwH0VTlzjyslgVGSv9GvVkWTTlO4Y6xQiOSJTWbZZ8Xs-YrTLmal9dbUrPZlv6Kxyeda3NQzg7fH86X_C-8gJ3SsRrjjz1YaLRjtMKx0rlZJQ6ZLSOvXBSW526MPAYLUVWBtKFoRMipTpIYexSXAE9gt2qrvwTYC6zyspcRFMfyyAXOk9E6jGs1B7NRTYdAx_4bVZdgg0zIM--mk4-huRjRGhQPmOYDkIxvymKQR_wj56vBxkaZDn9GLGVry8bQznx6cCfjsbwuBPudi4hlYeXCnuHnbS3dygxN3k507d_K-gyjcfnoZ1MtEzGcHBDpy090apQqiR--t9v9Qr2FqfHR-bow8mnZ3AH78gOIvccdtffL_0LjJnW6cv2m_gFJ4UUgg |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Regulation+of+peroxisomal+lipid+metabolism%3A+the+role+of+acyl-CoA+and+coenzyme+A+metabolizing+enzymes&rft.jtitle=Biochimie&rft.au=Hunt%2C+Mary+C&rft.au=Tillander%2C+Veronika&rft.au=Alexson%2C+Stefan+E+H&rft.date=2014-03-01&rft.eissn=1638-6183&rft.volume=98&rft.spage=45&rft_id=info:doi/10.1016%2Fj.biochi.2013.12.018&rft_id=info%3Apmid%2F24389458&rft.externalDocID=24389458 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0300-9084&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0300-9084&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0300-9084&client=summon |