Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosol
A novel lyase activity enzyme is characterized for the first time: HMG-CoA lyase-like1 (er-cHL), which is a close homolog of mitochondrial HMG-CoA lyase (mHL). Initial data show that there are nine mature transcripts for the novel gene HMGCLL1, although none of them has all its exons. The most abund...
Saved in:
Published in | Journal of lipid research Vol. 53; no. 10; pp. 2046 - 2056 |
---|---|
Main Authors | , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
01.10.2012
The American Society for Biochemistry and Molecular Biology Elsevier |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | A novel lyase activity enzyme is characterized for the first time: HMG-CoA lyase-like1 (er-cHL), which is a close homolog of mitochondrial HMG-CoA lyase (mHL). Initial data show that there are nine mature transcripts for the novel gene HMGCLL1, although none of them has all its exons. The most abundant transcript is called “variant b,” and it lacks exons 2 and 3. Moreover, a three-dimensional model of the novel enzyme is proposed. Colocalization studies show a dual location of the er-cHL in the endoplasmic reticulum (ER) and cytosol, but not in mitochondria or peroxisomes. Furthermore, the dissociation experiment suggests that it is a nonendoplasmic reticulum integral membrane protein. The kinetic parameters of er-cHL indicate that it has a lower Vmax and a higher substrate affinity than mHL. Protein expression and lyase activity were found in several tissues, and were particularly strong in lung and kidney. The occurrence of er-cHL in brain is surprising, as mHL has not been found there. Although mHL activity is clearly associated with energy metabolism, the results suggest that er-cHL is more closely related to another metabolic function, mostly at the pulmonary and brain level. |
---|---|
AbstractList | A novel lyase activity enzyme is characterized for the first time: HMG-CoA lyase-like1 (er-cHL), which is a close homolog of mitochondrial HMG-CoA lyase (mHL). Initial data show that there are nine mature transcripts for the novel gene HMGCLL1, although none of them has all its exons. The most abundant transcript is called "variant b," and it lacks exons 2 and 3. Moreover, a three-dimensional model of the novel enzyme is proposed. Colocalization studies show a dual location of the er-cHL in the endoplasmic reticulum (ER) and cytosol, but not in mitochondria or peroxisomes. Furthermore, the dissociation experiment suggests that it is a nonendoplasmic reticulum integral membrane protein. The kinetic parameters of er-cHL indicate that it has a lower V(max) and a higher substrate affinity than mHL. Protein expression and lyase activity were found in several tissues, and were particularly strong in lung and kidney. The occurrence of er-cHL in brain is surprising, as mHL has not been found there. Although mHL activity is clearly associated with energy metabolism, the results suggest that er-cHL is more closely related to another metabolic function, mostly at the pulmonary and brain level. A novel lyase activity enzyme is characterized for the first time: HMG-CoA lyase-like1 (er-cHL), which is a close homolog of mitochondrial HMG-CoA lyase (mHL). Initial data show that there are nine mature transcripts for the novel gene HMGCLL1, although none of them has all its exons. The most abundant transcript is called “variant b,” and it lacks exons 2 and 3. Moreover, a three-dimensional model of the novel enzyme is proposed. Colocalization studies show a dual location of the er-cHL in the endoplasmic reticulum (ER) and cytosol, but not in mitochondria or peroxisomes. Furthermore, the dissociation experiment suggests that it is a nonendoplasmic reticulum integral membrane protein. The kinetic parameters of er-cHL indicate that it has a lower Vmax and a higher substrate affinity than mHL. Protein expression and lyase activity were found in several tissues, and were particularly strong in lung and kidney. The occurrence of er-cHL in brain is surprising, as mHL has not been found there. Although mHL activity is clearly associated with energy metabolism, the results suggest that er-cHL is more closely related to another metabolic function, mostly at the pulmonary and brain level. A novel lyase activity enzyme is characterized for the first time: HMG-CoA lyase-like1 (er-cHL), which is a close homolog of mitochondrial HMG-CoA lyase (mHL). Initial data show that there are nine mature transcripts for the novel gene HMGCLL1 , although none of them has all its exons. The most abundant transcript is called “variant b,” and it lacks exons 2 and 3. Moreover, a three-dimensional model of the novel enzyme is proposed. Colocalization studies show a dual location of the er-cHL in the endoplasmic reticulum (ER) and cytosol, but not in mitochondria or peroxisomes. Furthermore, the dissociation experiment suggests that it is a nonendoplasmic reticulum integral membrane protein. The kinetic parameters of er-cHL indicate that it has a lower V max and a higher substrate affinity than mHL. Protein expression and lyase activity were found in several tissues, and were particularly strong in lung and kidney. The occurrence of er-cHL in brain is surprising, as mHL has not been found there. Although mHL activity is clearly associated with energy metabolism, the results suggest that er-cHL is more closely related to another metabolic function, mostly at the pulmonary and brain level. |
Author | López-Viñas, Eduardo Casals, Nuria Casale, César H. Hegardt, Fausto G. Gómez-Puertas, Paulino Pié, Juan Puisac, Beatriz Menao, Sebastián Teresa-Rodrigo, María E. Gil-Rodríguez, María C. Arnedo, María |
Author_xml | – sequence: 1 givenname: María surname: Arnedo fullname: Arnedo, María organization: Unit of Clinical Genetics and Functional Genomics, Department of Pharmacology and Physiology, School of Medicine, University of Zaragoza, Spain – sequence: 2 givenname: Sebastián surname: Menao fullname: Menao, Sebastián organization: Unit of Clinical Genetics and Functional Genomics, Department of Pharmacology and Physiology, School of Medicine, University of Zaragoza, Spain – sequence: 3 givenname: Beatriz surname: Puisac fullname: Puisac, Beatriz organization: Unit of Clinical Genetics and Functional Genomics, Department of Pharmacology and Physiology, School of Medicine, University of Zaragoza, Spain – sequence: 4 givenname: María E. surname: Teresa-Rodrigo fullname: Teresa-Rodrigo, María E. organization: Unit of Clinical Genetics and Functional Genomics, Department of Pharmacology and Physiology, School of Medicine, University of Zaragoza, Spain – sequence: 5 givenname: María C. surname: Gil-Rodríguez fullname: Gil-Rodríguez, María C. organization: Unit of Clinical Genetics and Functional Genomics, Department of Pharmacology and Physiology, School of Medicine, University of Zaragoza, Spain – sequence: 6 givenname: Eduardo surname: López-Viñas fullname: López-Viñas, Eduardo organization: Molecular Modeling Group, Centro de Biología Molecular “Severo Ochoa” (CSIC-UAM), Madrid, Spain – sequence: 7 givenname: Paulino surname: Gómez-Puertas fullname: Gómez-Puertas, Paulino organization: Molecular Modeling Group, Centro de Biología Molecular “Severo Ochoa” (CSIC-UAM), Madrid, Spain – sequence: 8 givenname: Nuria surname: Casals fullname: Casals, Nuria organization: Basic Sciences Department, Universitat Internacional de Catalunya, Catalunya, Spain – sequence: 9 givenname: César H. surname: Casale fullname: Casale, César H. organization: Department of Molecular Biology, National University of Río Cuarto, Río Cuarto, Argentina; and – sequence: 10 givenname: Fausto G. surname: Hegardt fullname: Hegardt, Fausto G. organization: Department of Biochemistry, School of Pharmacy, University of Barcelona, Barcelona, Spain – sequence: 11 givenname: Juan surname: Pié fullname: Pié, Juan email: juanpie@unizar.es organization: Unit of Clinical Genetics and Functional Genomics, Department of Pharmacology and Physiology, School of Medicine, University of Zaragoza, Spain |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22847177$$D View this record in MEDLINE/PubMed |
BookMark | eNptkUFr3DAQRkVJaTbbnnovPhaKU0mWLPtSCEubBBJ6yV2M5XFWiyxtJXvL5tdXrbehgZ5GaJ6ehvkuyJkPHgl5z-glY634vHPx8p5yqSh9RVZMVm2peM3PyIpSzkvOlTwnFyntKGVC1OwNOee8EYoptSK7zRYimAmjfYLJBl-EoYDChwO64ub-utyEq8IdIWGB_uk4YvHTTttM9DO4wgWzPLI-t_uwd5BGa4qIkzWzm8cCfF-Y4xRScG_J6wFcwnenuiYP374-bG7Ku-_Xt5uru9KItppKITAfsB4a2kguFAIw07VDMyDvWc85SlYDHWQ9IO0EVxykEpJR6GpV8WpNbhdtH2Cn99GOEI86gNV_LkJ81BDzeA61bIQYKPQqL09UnWhox1vKoeqpaASw7PqyuPZzN2Jv0E8R3Avpy463W_0YDroSlZRVkwUfT4IYfsyYJj3aZNA58BjmpBmtmpq2ba5r8mlBTQwpRRyev2FU_w5a56D1KehMf_h3smf2b7IZkAuAedUHi1EnY9Eb7G1EM-Vl2P-KfwFrc7hs |
CitedBy_id | crossref_primary_10_1016_j_scitotenv_2021_147130 crossref_primary_10_1038_s41375_018_0321_8 crossref_primary_10_1016_j_plantsci_2013_04_008 crossref_primary_10_1016_j_ymgme_2013_01_019 crossref_primary_10_1007_s40200_020_00566_5 crossref_primary_10_1074_jbc_RA119_008839 crossref_primary_10_1111_cen_13067 crossref_primary_10_3390_ijms20246124 |
Cites_doi | 10.1007/BF00208291 10.1016/S0021-9258(19)41601-3 10.1016/S1383-5742(98)00010-6 10.1016/j.neuroscience.2006.11.065 10.1023/A:1011029125228 10.1074/jbc.M304276200 10.1006/abbi.1997.0456 10.1074/jbc.M511346200 10.1093/bioinformatics/btq662 10.1016/S0022-2275(20)37733-6 10.1016/j.brainresrev.2008.09.002 10.1016/j.abb.2011.04.004 10.1093/nar/gkg520 10.1007/s004390000363 10.1016/S0021-9258(18)31784-8 10.1042/BJ20061313 10.1074/jbc.M506880200 10.1016/j.jsbmb.2005.10.005 10.1074/jbc.M304472200 10.1016/0005-2760(84)90167-X 10.1016/S0021-9258(19)81427-8 10.1042/bst0240274 10.1002/elps.1150181505 10.1042/bj3150071 10.1086/301730 10.1074/jbc.270.29.17311 10.1016/j.ymgme.2007.06.020 10.1016/0009-8981(76)90160-1 10.1074/jbc.M110.139931 10.1007/BF03179889 10.1016/S0021-9258(19)70410-4 10.1007/s11033-011-1270-8 10.1203/00006450-199607000-00023 10.1007/BF00966064 10.1007/s10545-010-9097-3 10.1016/S0968-0004(99)01427-9 10.1007/s10545-005-5518-0 10.1016/S0021-9258(17)36409-8 10.1111/j.1749-6632.1996.tb18614.x 10.1016/0009-8981(88)90294-X 10.1007/BF01800590 10.1016/S0003-9861(02)00584-2 10.1002/humu.20966 10.1074/jbc.271.40.24604 10.1016/j.plefa.2003.05.001 |
ContentType | Journal Article |
Copyright | 2012 © 2012 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. Copyright © 2012 by the American Society for Biochemistry and Molecular Biology, Inc. 2012 |
Copyright_xml | – notice: 2012 © 2012 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. – notice: Copyright © 2012 by the American Society for Biochemistry and Molecular Biology, Inc. 2012 |
DBID | 6I. AAFTH CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 5PM DOA |
DOI | 10.1194/jlr.M025700 |
DatabaseName | ScienceDirect Open Access Titles Elsevier:ScienceDirect:Open Access Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic PubMed Central (Full Participant titles) DOAJ Directory of Open Access Journals |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic |
DatabaseTitleList | MEDLINE |
Database_xml | – sequence: 1 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 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: 3 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 | Anatomy & Physiology Chemistry |
EISSN | 1539-7262 |
EndPage | 2056 |
ExternalDocumentID | oai_doaj_org_article_5844f0ad725743b480b2902a3d0484a1 10_1194_jlr_M025700 22847177 S0022227520431827 |
Genre | Research Support, Non-U.S. Gov't Journal Article |
GroupedDBID | --- -~X .55 .GJ 0SF 0VX 18M 29K 2WC 34G 39C 4.4 53G 5GY 5RE 5VS 6I. AAEDW AAFTH AAFWJ AAXUO AAYOK ABCQX ABOCM ACCCW ACGFO ACKIV ACNCT ACPRK ADBBV AENEX AEXQZ AFFNX AFOSN AFPKN AHPSJ AI. ALMA_UNASSIGNED_HOLDINGS AMRAJ AOIJS BAWUL BTFSW C1A CS3 D-I DIK DU5 E3Z EBS EJD F5P FDB FRP GROUPED_DOAJ GX1 H13 HH5 HYE H~9 J5H KQ8 L7B MVM OK1 P2P RHF RHI ROL RPM TBC TR2 TWZ VH1 W8F WH7 WOQ X7M XFK YHG YKV ZA5 ZGI ZXP ~KM 0R~ AALRI ADVLN AITUG AKRWK CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 5PM |
ID | FETCH-LOGICAL-c493t-44ec49e6f8085247eaa1cb9f8fe2d1d22e516a0f56fe0b4272a574510ab67323 |
IEDL.DBID | RPM |
ISSN | 0022-2275 |
IngestDate | Thu Jul 04 21:06:18 EDT 2024 Tue Sep 17 21:24:23 EDT 2024 Fri Aug 16 23:32:07 EDT 2024 Fri Aug 23 02:05:31 EDT 2024 Sat Sep 28 08:30:55 EDT 2024 Fri Feb 23 02:45:39 EST 2024 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 10 |
Keywords | lung mitochondrial HMG-CoA lyase liver lyase activity endoplasmic reticulum-cytosolic HMG-CoA lyase ketone bodies kinetics brain enzymology |
Language | English |
License | This is an open access article under the CC BY license. Creative Commons Attribution Non-Commercial License applies to Author Choice Articles Author's Choice—Final version full access. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c493t-44ec49e6f8085247eaa1cb9f8fe2d1d22e516a0f56fe0b4272a574510ab67323 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
OpenAccessLink | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3435538/ |
PMID | 22847177 |
PQID | 1038609910 |
PQPubID | 23479 |
PageCount | 11 |
ParticipantIDs | doaj_primary_oai_doaj_org_article_5844f0ad725743b480b2902a3d0484a1 pubmedcentral_primary_oai_pubmedcentral_nih_gov_3435538 proquest_miscellaneous_1038609910 crossref_primary_10_1194_jlr_M025700 pubmed_primary_22847177 elsevier_sciencedirect_doi_10_1194_jlr_M025700 |
PublicationCentury | 2000 |
PublicationDate | October 2012 2012-Oct 2012-10-00 20121001 2012-10-01 |
PublicationDateYYYYMMDD | 2012-10-01 |
PublicationDate_xml | – month: 10 year: 2012 text: October 2012 |
PublicationDecade | 2010 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States |
PublicationTitle | Journal of lipid research |
PublicationTitleAlternate | J Lipid Res |
PublicationYear | 2012 |
Publisher | Elsevier Inc The American Society for Biochemistry and Molecular Biology Elsevier |
Publisher_xml | – name: Elsevier Inc – name: The American Society for Biochemistry and Molecular Biology – name: Elsevier |
References | Casale, Alonso, Barra (bib23) 2001; 216 Kramer, Miziorko (bib5) 1980; 255 Rickers, Rininsland, Osborne, Reiss (bib33) 1994; 94 Casals, Gómez-Puertas, Pié, Mir, Roca, Puisac, Aledo, Clotet, Menao, Serra (bib10) 2003; 278 Clinkenbeard, Reed, Mooney, Lane (bib25) 1975; 250 Faull, Bolton, Halpern, Hammond, Danks (bib1) 1976; 73 Ashmarina, Robert, Elsliger, Mitchell (bib15) 1996; 315 Krisans (bib14) 1996; 804 Li, Sheng, Tang, Tsai-Morris, Dufau (bib32) 2006; 98 Fu, Runquist, Montgomery, Miziorko, Kim (bib4) 2010; 285 Roberts, Narasimhan, Miziorko (bib7) 1995; 270 Morris (bib39) 2005; 28 Guex, Diemand, Peitsch (bib17) 1999; 24 McGarry, Foster (bib45) 1969; 244 Roberts, Mitchell, Miziorko (bib8) 1996; 271 Tuinstra, Miziorko (bib9) 2003; 278 Strachan (bib29) 1992 Casale, Casals, Pié, Zapater, Pérez-Cerdá, Merinero, Martínez-Pardo, García-Peñas, García-Gonzalez, Lama (bib34) 1998; 349 Ashmarina, Rusnak, Miziorko, Mitchell (bib2) 1994; 269 Pié, Casals, Puisac, Hegardt (bib12) 2003; 59 Benkert, Biasini, Schewede (bib20) 2011; 27 Schwede, Kopp, Guex, Peitsch (bib19) 2003; 31 Montgomery, Miziorko (bib6) 2011; 511 Guex, Peitsch (bib21) 1997; 18 Menao, López-Viñas, Mir, Puisac, Gratacós, Arnedo, Carrasco, Moreno, Ramos, Gil (bib22) 2009; 30 Peitsch (bib18) 1996; 24 Fox, Hopkins, Cabacungan, Tildon (bib38) 1996; 40 Fu, Runquist, Forouhar, Hussain, Hunt, Miziorko, Kim (bib3) 2006; 281 Mitchell, Ozand, Robert, Ashmarina, Roberts, Gibson, Wanders, Wang, Chevalier, Plöchl (bib27) 1998; 62 Wanders, Shutgens, Zoeters (bib26) 1988; 171 Puisac, Ramos, Arnedo, Menao, Gil-Rodríguez, Teresa-Rodrigo, Pié, de Karam, Wesselink, Giménez (bib31) 2012; 39 Maalouf, Sullivan, Davis, Kim, Rho (bib42) 2007; 145 Harwood, Schneider, Stacpoole (bib37) 1984; 25 Guzmán, Blázquez (bib41) 2004; 70 Shah (bib46) 1982; 7 Callan, Bunning, Jones, High, Swanton (bib24) 2007; 401 Guo, Lukacik, Papagrigoriou, Meier, Lee, Adanski, Oppermann (bib36) 2006; 281 Bachhawat, Robinson, Coon (bib44) 1955; 216 Valentine (bib35) 1998; 411 Tuinstra, Burgner, Miziorko (bib16) 2002; 408 Ozand, al Aqeel, Gascon, Brismar, Thomas, Gleispach (bib28) 1991; 14 Maalouf, Rho, Mattson (bib43) 2009; 59 Pié, López-Viñas, Puisac, Menao, Pié, Casale, Ramos, Hegardt, Gómez-Puertas, Casals (bib13) 2007; 92 Lopes-Cardozo, Koper, Klein, Van Golde (bib40) 1984; 794 Muroi, Yorifuji, Uematsu, Shigematsu, Onigata, Maruyama, Nobutoki, Kitamura, Nakahata (bib30) 2000; 107 Puisac, Arnedo, Casale, Ribate, Castiella, Ramos, Ribes, Pérez-Cerdá, Casals, Hegardt (bib11) 2010; 33 Krisans (10.1194/jlr.M025700_bib14) 1996; 804 Guex (10.1194/jlr.M025700_bib17) 1999; 24 Guex (10.1194/jlr.M025700_bib21) 1997; 18 Rickers (10.1194/jlr.M025700_bib33) 1994; 94 Montgomery (10.1194/jlr.M025700_bib6) 2011; 511 Roberts (10.1194/jlr.M025700_bib8) 1996; 271 Pié (10.1194/jlr.M025700_bib13) 2007; 92 Puisac (10.1194/jlr.M025700_bib11) 2010; 33 Ashmarina (10.1194/jlr.M025700_bib15) 1996; 315 Callan (10.1194/jlr.M025700_bib24) 2007; 401 Casale (10.1194/jlr.M025700_bib34) 1998; 349 Fox (10.1194/jlr.M025700_bib38) 1996; 40 Menao (10.1194/jlr.M025700_bib22) 2009; 30 Puisac (10.1194/jlr.M025700_bib31) 2012; 39 Harwood (10.1194/jlr.M025700_bib37) 1984; 25 Tuinstra (10.1194/jlr.M025700_bib16) 2002; 408 Faull (10.1194/jlr.M025700_bib1) 1976; 73 Tuinstra (10.1194/jlr.M025700_bib9) 2003; 278 Schwede (10.1194/jlr.M025700_bib19) 2003; 31 Valentine (10.1194/jlr.M025700_bib35) 1998; 411 McGarry (10.1194/jlr.M025700_bib45) 1969; 244 Wanders (10.1194/jlr.M025700_bib26) 1988; 171 Maalouf (10.1194/jlr.M025700_bib42) 2007; 145 Ashmarina (10.1194/jlr.M025700_bib2) 1994; 269 Fu (10.1194/jlr.M025700_bib3) 2006; 281 Roberts (10.1194/jlr.M025700_bib7) 1995; 270 Mitchell (10.1194/jlr.M025700_bib27) 1998; 62 Shah (10.1194/jlr.M025700_bib46) 1982; 7 Clinkenbeard (10.1194/jlr.M025700_bib25) 1975; 250 Ozand (10.1194/jlr.M025700_bib28) 1991; 14 Muroi (10.1194/jlr.M025700_bib30) 2000; 107 Maalouf (10.1194/jlr.M025700_bib43) 2009; 59 Peitsch (10.1194/jlr.M025700_bib18) 1996; 24 Li (10.1194/jlr.M025700_bib32) 2006; 98 Benkert (10.1194/jlr.M025700_bib20) 2011; 27 Guzmán (10.1194/jlr.M025700_bib41) 2004; 70 Morris (10.1194/jlr.M025700_bib39) 2005; 28 Pié (10.1194/jlr.M025700_bib12) 2003; 59 Strachan (10.1194/jlr.M025700_bib29) 1992 Guo (10.1194/jlr.M025700_bib36) 2006; 281 Casals (10.1194/jlr.M025700_bib10) 2003; 278 Bachhawat (10.1194/jlr.M025700_bib44) 1955; 216 Lopes-Cardozo (10.1194/jlr.M025700_bib40) 1984; 794 Kramer (10.1194/jlr.M025700_bib5) 1980; 255 Fu (10.1194/jlr.M025700_bib4) 2010; 285 Casale (10.1194/jlr.M025700_bib23) 2001; 216 |
References_xml | – volume: 349 start-page: 129 year: 1998 end-page: 137 ident: bib34 article-title: A nonsense mutation in the exon 2 of the 3-hydroxy-3-methylglutaryl coenzyme A lyase (HL) gene producing three mature mRNAs is the main cause of 3-hydroxy-3-methylglutaric aciduria in European Mediterranean patients publication-title: Arch. Biochem. Biophys. contributor: fullname: Lama – volume: 401 start-page: 607 year: 2007 end-page: 612 ident: bib24 article-title: Biosynthesis of the dystonia-associated AAA+ ATPase torsinA at the endoplasmic reticulum publication-title: Biochem. J. contributor: fullname: Swanton – volume: 145 start-page: 256 year: 2007 end-page: 264 ident: bib42 article-title: Ketones inhibit mitochondrial production of reactive oxygen species production following glutamate excitotoxicity by increasing NADH oxidation publication-title: Neuroscience. contributor: fullname: Rho – volume: 794 start-page: 350 year: 1984 end-page: 352 ident: bib40 article-title: Acetoacetate is a cholesterogenic precursor for myelinating rat brain and spinal cord. Incorporation of label from [3–14C]acetoacetate, [14C]glucose and 3H2O publication-title: Biochim. Biophys. Acta. contributor: fullname: Van Golde – volume: 270 start-page: 17311 year: 1995 end-page: 17316 ident: bib7 article-title: Evaluation of cysteine 266 of human 3-hydroxy-3-methylglutaryl-CoA lyase as a catalytic residue publication-title: J. Biol. Chem. contributor: fullname: Miziorko – volume: 804 start-page: 142 year: 1996 end-page: 164 ident: bib14 article-title: Cell compartmentalization of cholesterol biosynthesis publication-title: Ann. N. Y. Acad. Sci. contributor: fullname: Krisans – volume: 70 start-page: 287 year: 2004 end-page: 292 ident: bib41 article-title: Ketone body synthesis in the brain: possible neuroprotective effects publication-title: Prostaglandins Leukot. Essent. Fatty Acids. contributor: fullname: Blázquez – volume: 216 start-page: 727 year: 1955 end-page: 736 ident: bib44 article-title: The enzymatic cleavage of beta-hydroxy-beta-methylglutaryl coenzyme A to acetoacetate and acetyl coenzyme A publication-title: J. Biol. Chem. contributor: fullname: Coon – volume: 33 start-page: 405 year: 2010 end-page: 410 ident: bib11 article-title: Differential HMG-CoA lyase expression in human tissues provides clues about 3-hydroxy-3-methylglutaric aciduria publication-title: J. Inherit. Metab. Dis. contributor: fullname: Hegardt – volume: 511 start-page: 48 year: 2011 end-page: 55 ident: bib6 article-title: Influence of multiple cysteines on human 3-hydroxy-3-methylglutaryl-CoA lyase activity and formation of inter-subunit adducts publication-title: Arch. Biochem. Biophys. contributor: fullname: Miziorko – volume: 18 start-page: 2714 year: 1997 end-page: 2723 ident: bib21 article-title: SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling publication-title: Electrophoresis. contributor: fullname: Peitsch – volume: 25 start-page: 967 year: 1984 end-page: 978 ident: bib37 article-title: Measurement of human leukocyte microsomal HMG-CoA reductase activity publication-title: J. Lipid Res. contributor: fullname: Stacpoole – year: 1992 ident: bib29 publication-title: The Human Genome. contributor: fullname: Strachan – volume: 250 start-page: 3108 year: 1975 end-page: 3116 ident: bib25 article-title: Intracellular localization of the 3-hydroxy-3-methylglutaryl coenzme A cycle enzymes in liver. Separate cytoplasmic and mitochondrial 3-hydroxy-3-methylglutaryl coenzyme A generating systems for cholesterogenesis and ketogenesis publication-title: J. Biol. Chem. contributor: fullname: Lane – volume: 98 start-page: 207 year: 2006 end-page: 217 ident: bib32 article-title: Tissue-cell- and species-specific expression of gonadotropinregulated long chain acyl-CoA synthetase (GR-LACS) in gonads, adrenal and brain. Identification of novel forms in the brain publication-title: J. Steroid Biochem. Mol. Biol. contributor: fullname: Dufau – volume: 255 start-page: 11023 year: 1980 end-page: 11028 ident: bib5 article-title: Purification and characterization of avian liver 3-hydroxy-3-methylglutaryl coenzyme A lyase publication-title: J. Biol. Chem. contributor: fullname: Miziorko – volume: 281 start-page: 7526 year: 2006 end-page: 7532 ident: bib3 article-title: Crystal structure of human 3-hydroxy-3-methylglutaryl-CoA Lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria publication-title: J. Biol. Chem. contributor: fullname: Kim – volume: 271 start-page: 24604 year: 1996 end-page: 24609 ident: bib8 article-title: Modeling of a mutation responsible for human 3-hydroxy-3-methylglutaryl-CoA lyase deficiency implicates histidine 233 as an active site residue publication-title: J. Biol. Chem. contributor: fullname: Miziorko – volume: 94 start-page: 311 year: 1994 end-page: 313 ident: bib33 article-title: Skipping of multiple CFTR exons is not a result of single exon omissions publication-title: Hum. Genet. contributor: fullname: Reiss – volume: 39 start-page: 4777 year: 2012 end-page: 4785 ident: bib31 article-title: Characterization of splice variants of the genes encoding human mitochondrial HMG-CoA lyase and HMG-CoA synthase, the main enzymes of the ketogenesis pathway publication-title: Mol. Biol. Rep. contributor: fullname: Giménez – volume: 14 start-page: 174 year: 1991 end-page: 188 ident: bib28 article-title: 3-Hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) lyase deficiency in Saudi Arabia publication-title: J. Inherit. Metab. Dis. contributor: fullname: Gleispach – volume: 107 start-page: 320 year: 2000 end-page: 326 ident: bib30 article-title: Molecular and clinical analysis of Japanese patients with 3-hydroxy-3-methylglutaryl CoA lyase (HL) deficiency publication-title: Hum. Genet. contributor: fullname: Nakahata – volume: 216 start-page: 85 year: 2001 end-page: 92 ident: bib23 article-title: Brain plasma membrane Na+,K+-ATPase is inhibited by acetylated tubulin publication-title: Mol. Cell. Biochem. contributor: fullname: Barra – volume: 269 start-page: 31929 year: 1994 end-page: 31932 ident: bib2 article-title: 3-Hydroxy-3-methylglutaryl-CoA lyase is present in mouse and human liver peroxisomes publication-title: J. Biol. Chem. contributor: fullname: Mitchell – volume: 62 start-page: 295 year: 1998 end-page: 300 ident: bib27 article-title: HMG CoA lyase deficiency: identification of five causal point mutations in codons 41 and 42, including a frequent Saudi Arabian mutation, R41Q publication-title: Am. J. Hum. Genet. contributor: fullname: Plöchl – volume: 411 start-page: 87 year: 1998 end-page: 117 ident: bib35 article-title: The association of nonsense codons with exon skipping publication-title: Mutat. Res. contributor: fullname: Valentine – volume: 40 start-page: 135 year: 1996 end-page: 141 ident: bib38 article-title: The role of glutamine and other alternate substrates as energy sources in the fetal rat lung type II cell publication-title: Pediatr. Res. contributor: fullname: Tildon – volume: 278 start-page: 37092 year: 2003 end-page: 37098 ident: bib9 article-title: Investigation of conserved acidic residues in 3-hydroxy-3-methylglutaryl-CoA lyase: implications for human disease and for functional roles in a family of related proteins publication-title: J. Biol. Chem. contributor: fullname: Miziorko – volume: 24 start-page: 364 year: 1999 end-page: 367 ident: bib17 article-title: Protein modelling for all publication-title: Trends Biochem. Sci. contributor: fullname: Peitsch – volume: 244 start-page: 4251 year: 1969 end-page: 4256 ident: bib45 article-title: Ketogenesis and cholesterol synthesis in normal and neoplastic tissues of the rat publication-title: J. Biol. Chem. contributor: fullname: Foster – volume: 30 start-page: E520 year: 2009 end-page: E529 ident: bib22 article-title: Ten novel HMGCL mutations in 24 patients of different origin with 3-hydroxy-3-methyl-glutaric aciduria publication-title: Hum. Mutat. contributor: fullname: Gil – volume: 92 start-page: 198 year: 2007 end-page: 209 ident: bib13 article-title: Molecular genetics of HMG-CoA lyase deficiency publication-title: Mol. Genet. Metab. contributor: fullname: Casals – volume: 315 start-page: 71 year: 1996 end-page: 75 ident: bib15 article-title: Characterization of the hydroxymethylglutaryl-CoA lyase precursor, a protein targeted to peroxisomes and mitochondria publication-title: Biochem. J. contributor: fullname: Mitchell – volume: 28 start-page: 109 year: 2005 end-page: 121 ident: bib39 article-title: Cerebral ketone body metabolism publication-title: J. Inherit. Metab. Dis. contributor: fullname: Morris – volume: 278 start-page: 29016 year: 2003 end-page: 29023 ident: bib10 article-title: Structural (betaalpha)8 TIM barrel model of 3-hydroxy-3-methylglutaryl-coenzyme A lyase publication-title: J. Biol. Chem. contributor: fullname: Serra – volume: 59 start-page: 311 year: 2003 end-page: 321 ident: bib12 article-title: Molecular basis of 3-hydroxy-3-methylglutaric aciduria publication-title: J. Physiol. Biochem. contributor: fullname: Hegardt – volume: 27 start-page: 343 year: 2011 end-page: 350 ident: bib20 article-title: Toward the estimation of the absolute quality of individual protein structure models publication-title: Bioinformatics. contributor: fullname: Schewede – volume: 59 start-page: 293 year: 2009 end-page: 315 ident: bib43 article-title: The neuroprotective properties of calorie restriction, the ketogenic diet, and ketone bodies publication-title: Brain Res. Rev. contributor: fullname: Mattson – volume: 24 start-page: 274 year: 1996 end-page: 279 ident: bib18 article-title: ProMod and Swiss-Model: internet-based tools for automated comparative protein modelling publication-title: Biochem. Soc. Trans. contributor: fullname: Peitsch – volume: 171 start-page: 95 year: 1988 end-page: 101 ident: bib26 article-title: 3-Hydroxy-3-methylglutaryl-CoA lyase in human skin fibroblasts: study of its properties and deficient activity in 3-hydroxy-3-methylglutaric aciduria patients using a simple spectrophotometric method publication-title: Clin. Chim. Acta. contributor: fullname: Zoeters – volume: 7 start-page: 1359 year: 1982 end-page: 1366 ident: bib46 article-title: Cytosolic 3-hydroxy-3-methyl glutaryl coenzyme a synthase in rat brain: properties and developmental change publication-title: Neurochem. Res. contributor: fullname: Shah – volume: 31 start-page: 3381 year: 2003 end-page: 3385 ident: bib19 article-title: SWISS-MODEL: an automated protein homology-modeling server publication-title: Nucleic Acids Res. contributor: fullname: Peitsch – volume: 281 start-page: 10291 year: 2006 end-page: 10297 ident: bib36 article-title: Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase publication-title: J. Biol. Chem. contributor: fullname: Oppermann – volume: 285 start-page: 26341 year: 2010 end-page: 26349 ident: bib4 article-title: Functional insights into human HMG-CoA lyase from structures of Acyl-CoA-containing ternary complexes publication-title: J. Biol. Chem. contributor: fullname: Kim – volume: 408 start-page: 286 year: 2002 end-page: 294 ident: bib16 article-title: Investigation of the oligomeric status of the peroxisomal isoform of human 3-hydroxy-3-methylglutaryl-CoA lyase publication-title: Arch. Biochem. Biophys. contributor: fullname: Miziorko – volume: 73 start-page: 553 year: 1976 end-page: 559 ident: bib1 article-title: The urinary organic acid profile associated with 3-hydroxy-3-methylglutaric aciduria publication-title: Clin. Chim. Acta. contributor: fullname: Danks – volume: 94 start-page: 311 year: 1994 ident: 10.1194/jlr.M025700_bib33 article-title: Skipping of multiple CFTR exons is not a result of single exon omissions publication-title: Hum. Genet. doi: 10.1007/BF00208291 contributor: fullname: Rickers – volume: 250 start-page: 3108 year: 1975 ident: 10.1194/jlr.M025700_bib25 article-title: Intracellular localization of the 3-hydroxy-3-methylglutaryl coenzme A cycle enzymes in liver. Separate cytoplasmic and mitochondrial 3-hydroxy-3-methylglutaryl coenzyme A generating systems for cholesterogenesis and ketogenesis publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)41601-3 contributor: fullname: Clinkenbeard – volume: 411 start-page: 87 year: 1998 ident: 10.1194/jlr.M025700_bib35 article-title: The association of nonsense codons with exon skipping publication-title: Mutat. Res. doi: 10.1016/S1383-5742(98)00010-6 contributor: fullname: Valentine – volume: 145 start-page: 256 year: 2007 ident: 10.1194/jlr.M025700_bib42 article-title: Ketones inhibit mitochondrial production of reactive oxygen species production following glutamate excitotoxicity by increasing NADH oxidation publication-title: Neuroscience. doi: 10.1016/j.neuroscience.2006.11.065 contributor: fullname: Maalouf – volume: 216 start-page: 85 year: 2001 ident: 10.1194/jlr.M025700_bib23 article-title: Brain plasma membrane Na+,K+-ATPase is inhibited by acetylated tubulin publication-title: Mol. Cell. Biochem. doi: 10.1023/A:1011029125228 contributor: fullname: Casale – volume: 278 start-page: 29016 year: 2003 ident: 10.1194/jlr.M025700_bib10 article-title: Structural (betaalpha)8 TIM barrel model of 3-hydroxy-3-methylglutaryl-coenzyme A lyase publication-title: J. Biol. Chem. doi: 10.1074/jbc.M304276200 contributor: fullname: Casals – volume: 349 start-page: 129 year: 1998 ident: 10.1194/jlr.M025700_bib34 article-title: A nonsense mutation in the exon 2 of the 3-hydroxy-3-methylglutaryl coenzyme A lyase (HL) gene producing three mature mRNAs is the main cause of 3-hydroxy-3-methylglutaric aciduria in European Mediterranean patients publication-title: Arch. Biochem. Biophys. doi: 10.1006/abbi.1997.0456 contributor: fullname: Casale – volume: 281 start-page: 10291 year: 2006 ident: 10.1194/jlr.M025700_bib36 article-title: Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase publication-title: J. Biol. Chem. doi: 10.1074/jbc.M511346200 contributor: fullname: Guo – volume: 27 start-page: 343 year: 2011 ident: 10.1194/jlr.M025700_bib20 article-title: Toward the estimation of the absolute quality of individual protein structure models publication-title: Bioinformatics. doi: 10.1093/bioinformatics/btq662 contributor: fullname: Benkert – volume: 25 start-page: 967 year: 1984 ident: 10.1194/jlr.M025700_bib37 article-title: Measurement of human leukocyte microsomal HMG-CoA reductase activity publication-title: J. Lipid Res. doi: 10.1016/S0022-2275(20)37733-6 contributor: fullname: Harwood – volume: 59 start-page: 293 year: 2009 ident: 10.1194/jlr.M025700_bib43 article-title: The neuroprotective properties of calorie restriction, the ketogenic diet, and ketone bodies publication-title: Brain Res. Rev. doi: 10.1016/j.brainresrev.2008.09.002 contributor: fullname: Maalouf – volume: 511 start-page: 48 year: 2011 ident: 10.1194/jlr.M025700_bib6 article-title: Influence of multiple cysteines on human 3-hydroxy-3-methylglutaryl-CoA lyase activity and formation of inter-subunit adducts publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2011.04.004 contributor: fullname: Montgomery – volume: 31 start-page: 3381 year: 2003 ident: 10.1194/jlr.M025700_bib19 article-title: SWISS-MODEL: an automated protein homology-modeling server publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkg520 contributor: fullname: Schwede – volume: 107 start-page: 320 year: 2000 ident: 10.1194/jlr.M025700_bib30 article-title: Molecular and clinical analysis of Japanese patients with 3-hydroxy-3-methylglutaryl CoA lyase (HL) deficiency publication-title: Hum. Genet. doi: 10.1007/s004390000363 contributor: fullname: Muroi – volume: 269 start-page: 31929 year: 1994 ident: 10.1194/jlr.M025700_bib2 article-title: 3-Hydroxy-3-methylglutaryl-CoA lyase is present in mouse and human liver peroxisomes publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)31784-8 contributor: fullname: Ashmarina – volume: 401 start-page: 607 year: 2007 ident: 10.1194/jlr.M025700_bib24 article-title: Biosynthesis of the dystonia-associated AAA+ ATPase torsinA at the endoplasmic reticulum publication-title: Biochem. J. doi: 10.1042/BJ20061313 contributor: fullname: Callan – volume: 281 start-page: 7526 year: 2006 ident: 10.1194/jlr.M025700_bib3 article-title: Crystal structure of human 3-hydroxy-3-methylglutaryl-CoA Lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria publication-title: J. Biol. Chem. doi: 10.1074/jbc.M506880200 contributor: fullname: Fu – volume: 98 start-page: 207 year: 2006 ident: 10.1194/jlr.M025700_bib32 article-title: Tissue-cell- and species-specific expression of gonadotropinregulated long chain acyl-CoA synthetase (GR-LACS) in gonads, adrenal and brain. Identification of novel forms in the brain publication-title: J. Steroid Biochem. Mol. Biol. doi: 10.1016/j.jsbmb.2005.10.005 contributor: fullname: Li – volume: 278 start-page: 37092 year: 2003 ident: 10.1194/jlr.M025700_bib9 article-title: Investigation of conserved acidic residues in 3-hydroxy-3-methylglutaryl-CoA lyase: implications for human disease and for functional roles in a family of related proteins publication-title: J. Biol. Chem. doi: 10.1074/jbc.M304472200 contributor: fullname: Tuinstra – volume: 794 start-page: 350 year: 1984 ident: 10.1194/jlr.M025700_bib40 article-title: Acetoacetate is a cholesterogenic precursor for myelinating rat brain and spinal cord. Incorporation of label from [3–14C]acetoacetate, [14C]glucose and 3H2O publication-title: Biochim. Biophys. Acta. doi: 10.1016/0005-2760(84)90167-X contributor: fullname: Lopes-Cardozo – volume: 216 start-page: 727 year: 1955 ident: 10.1194/jlr.M025700_bib44 article-title: The enzymatic cleavage of beta-hydroxy-beta-methylglutaryl coenzyme A to acetoacetate and acetyl coenzyme A publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)81427-8 contributor: fullname: Bachhawat – year: 1992 ident: 10.1194/jlr.M025700_bib29 contributor: fullname: Strachan – volume: 24 start-page: 274 year: 1996 ident: 10.1194/jlr.M025700_bib18 article-title: ProMod and Swiss-Model: internet-based tools for automated comparative protein modelling publication-title: Biochem. Soc. Trans. doi: 10.1042/bst0240274 contributor: fullname: Peitsch – volume: 18 start-page: 2714 year: 1997 ident: 10.1194/jlr.M025700_bib21 article-title: SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling publication-title: Electrophoresis. doi: 10.1002/elps.1150181505 contributor: fullname: Guex – volume: 315 start-page: 71 year: 1996 ident: 10.1194/jlr.M025700_bib15 article-title: Characterization of the hydroxymethylglutaryl-CoA lyase precursor, a protein targeted to peroxisomes and mitochondria publication-title: Biochem. J. doi: 10.1042/bj3150071 contributor: fullname: Ashmarina – volume: 62 start-page: 295 year: 1998 ident: 10.1194/jlr.M025700_bib27 article-title: HMG CoA lyase deficiency: identification of five causal point mutations in codons 41 and 42, including a frequent Saudi Arabian mutation, R41Q publication-title: Am. J. Hum. Genet. doi: 10.1086/301730 contributor: fullname: Mitchell – volume: 270 start-page: 17311 year: 1995 ident: 10.1194/jlr.M025700_bib7 article-title: Evaluation of cysteine 266 of human 3-hydroxy-3-methylglutaryl-CoA lyase as a catalytic residue publication-title: J. Biol. Chem. doi: 10.1074/jbc.270.29.17311 contributor: fullname: Roberts – volume: 92 start-page: 198 year: 2007 ident: 10.1194/jlr.M025700_bib13 article-title: Molecular genetics of HMG-CoA lyase deficiency publication-title: Mol. Genet. Metab. doi: 10.1016/j.ymgme.2007.06.020 contributor: fullname: Pié – volume: 73 start-page: 553 year: 1976 ident: 10.1194/jlr.M025700_bib1 article-title: The urinary organic acid profile associated with 3-hydroxy-3-methylglutaric aciduria publication-title: Clin. Chim. Acta. doi: 10.1016/0009-8981(76)90160-1 contributor: fullname: Faull – volume: 285 start-page: 26341 year: 2010 ident: 10.1194/jlr.M025700_bib4 article-title: Functional insights into human HMG-CoA lyase from structures of Acyl-CoA-containing ternary complexes publication-title: J. Biol. Chem. doi: 10.1074/jbc.M110.139931 contributor: fullname: Fu – volume: 59 start-page: 311 year: 2003 ident: 10.1194/jlr.M025700_bib12 article-title: Molecular basis of 3-hydroxy-3-methylglutaric aciduria publication-title: J. Physiol. Biochem. doi: 10.1007/BF03179889 contributor: fullname: Pié – volume: 255 start-page: 11023 year: 1980 ident: 10.1194/jlr.M025700_bib5 article-title: Purification and characterization of avian liver 3-hydroxy-3-methylglutaryl coenzyme A lyase publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)70410-4 contributor: fullname: Kramer – volume: 39 start-page: 4777 year: 2012 ident: 10.1194/jlr.M025700_bib31 article-title: Characterization of splice variants of the genes encoding human mitochondrial HMG-CoA lyase and HMG-CoA synthase, the main enzymes of the ketogenesis pathway publication-title: Mol. Biol. Rep. doi: 10.1007/s11033-011-1270-8 contributor: fullname: Puisac – volume: 40 start-page: 135 year: 1996 ident: 10.1194/jlr.M025700_bib38 article-title: The role of glutamine and other alternate substrates as energy sources in the fetal rat lung type II cell publication-title: Pediatr. Res. doi: 10.1203/00006450-199607000-00023 contributor: fullname: Fox – volume: 7 start-page: 1359 year: 1982 ident: 10.1194/jlr.M025700_bib46 article-title: Cytosolic 3-hydroxy-3-methyl glutaryl coenzyme a synthase in rat brain: properties and developmental change publication-title: Neurochem. Res. doi: 10.1007/BF00966064 contributor: fullname: Shah – volume: 33 start-page: 405 year: 2010 ident: 10.1194/jlr.M025700_bib11 article-title: Differential HMG-CoA lyase expression in human tissues provides clues about 3-hydroxy-3-methylglutaric aciduria publication-title: J. Inherit. Metab. Dis. doi: 10.1007/s10545-010-9097-3 contributor: fullname: Puisac – volume: 24 start-page: 364 year: 1999 ident: 10.1194/jlr.M025700_bib17 article-title: Protein modelling for all publication-title: Trends Biochem. Sci. doi: 10.1016/S0968-0004(99)01427-9 contributor: fullname: Guex – volume: 28 start-page: 109 year: 2005 ident: 10.1194/jlr.M025700_bib39 article-title: Cerebral ketone body metabolism publication-title: J. Inherit. Metab. Dis. doi: 10.1007/s10545-005-5518-0 contributor: fullname: Morris – volume: 244 start-page: 4251 year: 1969 ident: 10.1194/jlr.M025700_bib45 article-title: Ketogenesis and cholesterol synthesis in normal and neoplastic tissues of the rat publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)36409-8 contributor: fullname: McGarry – volume: 804 start-page: 142 year: 1996 ident: 10.1194/jlr.M025700_bib14 article-title: Cell compartmentalization of cholesterol biosynthesis publication-title: Ann. N. Y. Acad. Sci. doi: 10.1111/j.1749-6632.1996.tb18614.x contributor: fullname: Krisans – volume: 171 start-page: 95 year: 1988 ident: 10.1194/jlr.M025700_bib26 article-title: 3-Hydroxy-3-methylglutaryl-CoA lyase in human skin fibroblasts: study of its properties and deficient activity in 3-hydroxy-3-methylglutaric aciduria patients using a simple spectrophotometric method publication-title: Clin. Chim. Acta. doi: 10.1016/0009-8981(88)90294-X contributor: fullname: Wanders – volume: 14 start-page: 174 year: 1991 ident: 10.1194/jlr.M025700_bib28 article-title: 3-Hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) lyase deficiency in Saudi Arabia publication-title: J. Inherit. Metab. Dis. doi: 10.1007/BF01800590 contributor: fullname: Ozand – volume: 408 start-page: 286 year: 2002 ident: 10.1194/jlr.M025700_bib16 article-title: Investigation of the oligomeric status of the peroxisomal isoform of human 3-hydroxy-3-methylglutaryl-CoA lyase publication-title: Arch. Biochem. Biophys. doi: 10.1016/S0003-9861(02)00584-2 contributor: fullname: Tuinstra – volume: 30 start-page: E520 year: 2009 ident: 10.1194/jlr.M025700_bib22 article-title: Ten novel HMGCL mutations in 24 patients of different origin with 3-hydroxy-3-methyl-glutaric aciduria publication-title: Hum. Mutat. doi: 10.1002/humu.20966 contributor: fullname: Menao – volume: 271 start-page: 24604 year: 1996 ident: 10.1194/jlr.M025700_bib8 article-title: Modeling of a mutation responsible for human 3-hydroxy-3-methylglutaryl-CoA lyase deficiency implicates histidine 233 as an active site residue publication-title: J. Biol. Chem. doi: 10.1074/jbc.271.40.24604 contributor: fullname: Roberts – volume: 70 start-page: 287 year: 2004 ident: 10.1194/jlr.M025700_bib41 article-title: Ketone body synthesis in the brain: possible neuroprotective effects publication-title: Prostaglandins Leukot. Essent. Fatty Acids. doi: 10.1016/j.plefa.2003.05.001 contributor: fullname: Guzmán |
SSID | ssj0014461 |
Score | 2.1341164 |
Snippet | A novel lyase activity enzyme is characterized for the first time: HMG-CoA lyase-like1 (er-cHL), which is a close homolog of mitochondrial HMG-CoA lyase (mHL).... |
SourceID | doaj pubmedcentral proquest crossref pubmed elsevier |
SourceType | Open Website Open Access Repository Aggregation Database Index Database Publisher |
StartPage | 2046 |
SubjectTerms | Amino Acid Sequence brain Cytosol - enzymology Cytosol - metabolism Endoplasmic Reticulum - enzymology Endoplasmic Reticulum - metabolism endoplasmic reticulum-cytosolic HMG-CoA lyase enzymology HEK293 Cells Humans ketone bodies kinetics liver lung lyase activity Mitochondria - enzymology Mitochondria - metabolism mitochondrial HMG-CoA lyase Molecular Sequence Data Oxo-Acid-Lyases - analysis Oxo-Acid-Lyases - chemistry Oxo-Acid-Lyases - genetics Peroxisomes - enzymology Peroxisomes - metabolism Protein Splicing |
SummonAdditionalLinks | – databaseName: DOAJ Directory of Open Access Journals dbid: DOA link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3Pa9swGBWll_VStnbtsl9oUHZzq1-W7GMW1oVBd2qhNyHZEk1J5NKmg-yv3yfJDnU32GU3Eyu27PfEe5_86RNCJ4rQylUtLWpDeAGKVxZWNWUhuVCORoHO2RY_5PxKfL8ur59s9RVzwnJ54PzizkAghSemVcAtwa2oiGU1YYa3wD1hcuBDyyGY6r8fQJBDhzrhjKmyX5kHEfvZ7fL-9ILEzdvISItSyf6RJP1pOZ9nTj6RovOXaL_3kHia-_4K7bhwgA6nAeLn1QZ_ximrM02XH6AXs2FHt0N0O9tWZ86LL3HnscGh--mWeH7xrZh1U7zcgK5hF35tVg7HWVpoEddr4ah66U-LAKfb7g5892rR4LQMMs4hYhNa3GzWHdD5Nbo8_3o5mxf9XgtFI2q-LoRwcOCkr8CDMcDJGNrY2lfesZa2jLmSSkN8Kb0jVjDFDOABA9pYqTjjR2g3dMG9QdgZLrmKHPBwHVtXpTemth5glA1j1QSdDC9d3-WKGjpFIrXQgI3usZmgLxGQbZNYBjv9AOTQPTn0v8gxQacDnLp3FNkpwKUWf7_rpwF0DeDEjycmuO7xQcdC8hLsNIU2x5kE276xpPFKTZAa0WPU-fGZsLhJtbw5jAbQnLf_42nfoT2wcyynGr5Hu-v7R_cBLNPafkyj4zfiXxEq priority: 102 providerName: Directory of Open Access Journals |
Title | Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosol |
URI | https://dx.doi.org/10.1194/jlr.M025700 https://www.ncbi.nlm.nih.gov/pubmed/22847177 https://search.proquest.com/docview/1038609910 https://pubmed.ncbi.nlm.nih.gov/PMC3435538 https://doaj.org/article/5844f0ad725743b480b2902a3d0484a1 |
Volume | 53 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3db9MwED9t4wFeJtj46IDKSBNvaRPbiZPHEjEqpiIEQ0xCKLITG4IapyodUvnrOTtJRYEn3qLEdizf2fe7830AnIswSnVaRUEmQxagxIsDJco4SBgXOnICuvO2eJPMP_DX1_H1AcRDLIx32i9VPbHLZmLrr963ctWU08FPbPp2kTMcAjfq9BAOBWODit5fHaB-Ew0pwikVcR-Uh8r69NtyPVmErm6bKwBH_cksxJ5E8on79wTT38DzT__J3wTSxV047pEkmXUzvgcH2p7A6cyiFt1syXPifTu90fwEbudDXbdTaPJdjuYuBJO0hkhi2x96SeaLV0Hezshyi9KNaPtz22jibLXYwkVtESf7fKfa4ueqXSH6buqS-GBIZ0kk0lak3G5aZOpP7z_fh6uLl1f5POiLLgQlz9gm4Fzjg05MimCMIsGkjEqVmdRoWkUVpTqOEhmaODE6VJwKKmPBcWdLlQhG2QM4sq3Vj4BoyRImHDMYHEdlaWykzJTh3CQlLv4Izod1L1Zdao3CqyQZL5BSRU-pEbxwNNk1cfmw_Yt2_aXouaJAGMVNKCuBXThTPA0VzUIqWYUnFJfRCCYDRYseWnSQAYeq__3XZwPdC6SPu0WRVrc33wuXUT5BXB1hm4cdH-zmNrDUCMQeh-xNfv8L8rhP6t3z9Nl_93wMdxDM0c7R8AkcbdY3-ikCpo0aw63Z5buPl2NvcBj77fILCasW0Q |
link.rule.ids | 230,315,733,786,790,870,891,2115,27957,27958,53827,53829 |
linkProvider | National Library of Medicine |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3db9MwELfGeBgvfGwwyqeRJt6SJrYTJ48lYhRYJyQKmoRQZCc2BBqnKilS99dzdpKKDl7gKVH8kUT3s-939t0ZoRMehIlKytBLRUA90HiRJ3kReTFlXIVWQXfeFufx9AN7cxFd7KFoiIVxTvuFrHyzqH1TfXW-lcu6GA9-YuN3s4xCFzBQx9fQdbgQPhjp_eYBWDjhkCScEB71YXlgro-_LVb-LLAnt9kj4Iibmznf0Ukudf-OavqTel71oPxNJZ3eQh-Hn-k8Ub7761b6xeWVPI___Le30c2epOJJV3wH7SlziI4mBgz0eoOfY-c26tbjD9FBNhwZd4TqbJv-uYvuxI3GApvmp1rg6eyVlzUTvNiA4sTKXG5qhe0yMNSwAWHYqlXXqDJQXDZLIPZ1VWAXZ2kXKbEwJS42bQPj5dP7z3fR_PTlPJt6_XkOXsFS2nqMKbhRsU6A5xHAghBhIVOdaEXKsCRERWEsAh3FWgWSEU5ExBlMGkLGnBJ6D-2bxqj7CCtBY8otzjT0I9Mk0kKkUjOm4wKkOkIng0DzZZe1I3fWTspygEDeQ2CEXlhhb6vYVNvuQbP6kvciyIGhMR2IkkMTRiVLAknSgAhawuTHRDhC_gCVvGctHRuBrqq_v_XZAKgc5GM3aIRRzfpHbpPVx0DZQ6hz3AFs-20DVkeI70Bv5-N3SwBQLl94D6AH_93yKTqYzmdn-dnr87cP0Q3gjKTzZ3yE9tvVWj0GXtbKJ24U_gJCYDYw |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Zb9QwELagSMALR8uxnEaqeMvlOHHyuASW5diqEkWqQCiyExsCG2e1ZJG2v56xk6yawlPfrPiIo_ns-cYZzyB0yPwgkUkZOCn3Qwc0XuQIVkROHFImA6OgO2-Lo3j-mb4_jU7PpfqyTvuFqFy9rF1d_bC-lau68AY_Me94kYUwBCxUb1Uq7yq6BkWSDoZ6_wMBrJxgCBROCIv6q3lgsns_l2t34ZvsbSYNHLH7M2MjvWTD94_U07_086IX5Tm1NLuNvgwf1Hmj_HI3rXCLswuxHi_1xXfQrZ6s4mnX5C66IvU-OphqMNTrLX6JrfuoPZffRzeyIXXcAaqzXRjo7pYnbhTmWDd_5BLPF2-drJni5RYUKJb6bFtLbI6DoYW5GIaNerWdKg3VZbMCgl9XBbb3Lc1hJea6xMW2bWDdfP307R46mb05yeZOn9fBKWgatg6lEgoyVgnwPQKY4DwoRKoSJUkZlITIKIi5r6JYSV9QwgiPGIXNg4uYhSS8j_Z0o-VDhCUP45AZvCkYR6RJpDhPhaJUxQVIdoIOB6Hmqy56R26tnpTmAIO8h8EEvTIC3zUxIbftg2b9Pe_FkANTo8rnJYMuNBQ08QVJfcLDEjZByoMJcge45D176VgJDFX9_60vBlDlIB_zo4Zr2Wx-5yZofQzUPYA2DzqQ7eY24HWC2Ah-o8mPawBUNm54D6JHl-75HF0_fj3LP747-vAY3QTqSDq3xidor11v5FOgZ614ZhfiX-qrOLA |
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=Characterization+of+a+novel+HMG-CoA+lyase+enzyme+with+a+dual+location+in+endoplasmic+reticulum+and+cytosol&rft.jtitle=Journal+of+lipid+research&rft.au=Arnedo%2C+Mar%C3%ADa&rft.au=Menao%2C+Sebasti%C3%A1n&rft.au=Puisac%2C+Beatriz&rft.au=Teresa-Rodrigo%2C+Mar%C3%ADa+E.&rft.date=2012-10-01&rft.pub=Elsevier+Inc&rft.issn=0022-2275&rft.eissn=1539-7262&rft.volume=53&rft.issue=10&rft.spage=2046&rft.epage=2056&rft_id=info:doi/10.1194%2Fjlr.M025700&rft.externalDocID=S0022227520431827 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0022-2275&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0022-2275&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0022-2275&client=summon |