Cyclization characteristics of cyclodextrin glucanotransferase are conferred by the NH2-terminal region of the enzyme
Classifications Services AEM Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue AEM About AEM Subscribers Authors Reviewers Advertisers Inquiries from the...
Saved in:
Published in | Applied and Environmental Microbiology Vol. 58; no. 12; pp. 4016 - 4025 |
---|---|
Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Society for Microbiology
01.12.1992
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Classifications
Services
AEM
Citing Articles
Google Scholar
PubMed
Related Content
Social Bookmarking
CiteULike
Delicious
Digg
Facebook
Google+
Mendeley
Reddit
StumbleUpon
Twitter
current issue
Spotlights in the Current Issue
AEM
About
AEM
Subscribers
Authors
Reviewers
Advertisers
Inquiries from the Press
Permissions & Commercial Reprints
ASM Journals Public Access Policy
AEM
RSS Feeds
1752 N Street N.W. • Washington DC 20036
202.737.3600 • 202.942.9355 fax • journals@asmusa.org
Print ISSN:
0099-2240
Online ISSN:
1098-5336
Copyright © 2014
by the
American Society for Microbiology.
For an alternate route to
AEM
.asm.org, visit:
AEM
|
---|---|
AbstractList | Cyclodextrin glucanotransferase (CGTase; EC 2.4.1.19) is produced mainly by Bacillus strains. CGTase from Bacillus macerans IFO3490 produces alpha-cyclodextrin as the major hydrolysis product from starch, whereas thermostable CGTase from Bacillus stearothermophilus NO2 produces alpha- and beta-cyclodextrins. To analyze the cyclization characteristics of CGTase, we cloned different types of CGTase genes and constructed chimeric genes. CGTase genes from these two strains were cloned in Bacillus subtilis NA-1 by using pTB523 as a vector plasmid, and their nucleotide sequences were determined. Three CGTase genes (cgt-1, cgt-5, and cgt-232) were isolated from B. stearothermophilus NO2. Nucleotide sequence analysis revealed that the three CGTase genes have different nucleotide sequences encoding the same amino acid sequence. Base substitutions were found at the third letter of five codons among the three genes. Each open reading frame was composed of 2,133 bases, encoding 711 amino acids containing 31 amino acids as a signal sequence. The molecular weight of the mature enzyme was estimated to be 75,374. The CGTase gene (cgtM) of B. macerans IFO3490 was composed of 2,142 bases, encoding 714 amino acids containing 27 residues as a signal sequence. The molecular weight of the mature enzyme was estimated to be 74,008. The sequence determined in this work was quite different from that reported previously by other workers. From data on the three-dimensional structure of a CGTase, seven kinds of chimeric CGTase genes were constructed by using cgt-1 from B. stearothermophilus NO2 and cgtM from B. macerans IFO3490. We examined the characteristics of these chimeric enzymes on cyclodextrin production and thermostability. It was found that the cyclization reaction was conferred by the NH2-terminal region of CGTase and that the thermostability of some chimeric enzymes was lower than that of the parental CGTases. Classifications Services AEM Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue AEM About AEM Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy AEM RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0099-2240 Online ISSN: 1098-5336 Copyright © 2014 by the American Society for Microbiology. For an alternate route to AEM .asm.org, visit: AEM |
Author | T Imanaka K B Woo A Lejeune M Kanemoto H Kakihara S Fujiwara K Sakaguchi |
AuthorAffiliation | Department of Biotechnology, Faculty of Engineering, Osaka University, Japan |
AuthorAffiliation_xml | – name: Department of Biotechnology, Faculty of Engineering, Osaka University, Japan |
Author_xml | – sequence: 1 givenname: S surname: Fujiwara fullname: Fujiwara, S organization: Department of Biotechnology, Faculty of Engineering, Osaka University, Japan – sequence: 2 givenname: H surname: Kakihara fullname: Kakihara, H – sequence: 3 givenname: K B surname: Woo fullname: Woo, K B – sequence: 4 givenname: A surname: Lejeune fullname: Lejeune, A – sequence: 5 givenname: M surname: Kanemoto fullname: Kanemoto, M – sequence: 6 givenname: K surname: Sakaguchi fullname: Sakaguchi, K – sequence: 7 givenname: T surname: Imanaka fullname: Imanaka, T |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/1476442$$D View this record in MEDLINE/PubMed |
BookMark | eNpdkcFu1DAQhi1UVLaFR0CyOHBLmLGdrH3ggFZAK1VwgbPleicbo8QudgJsn55EW0HhZI3--T-P9F2ws5giMcYRakSh3zga60bXKGoF2FYKRFOjMeIJ2yAYXTVStmdsA2BMJYSCZ-yilG8AoKDV5-wc1bZVSmzYvDv6Idy7KaTIfe-y8xPlUKbgC08d90uc9vRryiHywzB7F9OUXSwdZVeIu0zcp7hMmfb89sinnvinK1EtlDFEN_BMh5W9sNaI4v1xpOfsaeeGQi8e3kv29cP7L7ur6ubzx-vdu5vKN0ZPlW5kK1vyoBxKAK1NA3JPQiMZrw04QNp6BJTYIHZkhDNqK6RuGyStSF6ytyfu3Xw70t5TXG4f7F0Oo8tHm1yw_yYx9PaQfljUUqBZ-q8f-jl9n6lMdgzF0zC4SGkudiuVkC3CsqhPiz6nUjJ1f_5AsKsxuxizjbYo7GrMrsbsamypvnx849_iSdGSvzrlfTj0P0Mm68r4H07-BiC6ojQ |
CitedBy_id | crossref_primary_10_1515_biolog_2015_0087 crossref_primary_10_1111_j_1742_4658_2007_05649_x crossref_primary_10_1016_0167_4838_94_00214_2 crossref_primary_10_1128_AEM_65_5_1991_1997_1999 crossref_primary_10_1016_S0079_6107_97_00015_1 crossref_primary_10_1016_j_biotechadv_2013_12_004 crossref_primary_10_1016_j_enzmictec_2011_12_001 crossref_primary_10_1007_s00253_009_1988_6 crossref_primary_10_1128_jb_175_17_5452_5459_1993 crossref_primary_10_1016_j_jbiosc_2015_04_013 crossref_primary_10_1111_j_1574_6968_1998_tb13117_x crossref_primary_10_1016_j_tifs_2013_11_005 crossref_primary_10_5458_jag_54_109 crossref_primary_10_1007_BF00128597 crossref_primary_10_1016_j_fob_2015_06_002 crossref_primary_10_1016_S1389_1723_99_80114_5 crossref_primary_10_1016_0378_1119_94_90826_5 crossref_primary_10_1128_AEM_66_7_3058_3064_2000 crossref_primary_10_1590_0001_3765201920180568 crossref_primary_10_1016_j_ijbiomac_2020_09_103 crossref_primary_10_1186_s12896_018_0463_9 crossref_primary_10_1016_S0014_5793_97_01192_7 crossref_primary_10_1007_BF00023233 crossref_primary_10_1016_j_carres_2006_06_024 crossref_primary_10_1080_10408399509527706 crossref_primary_10_1021_jf010928q crossref_primary_10_1002_jobm_3620360507 crossref_primary_10_5352_JLS_2004_14_3_391 crossref_primary_10_1002_star_201700016 crossref_primary_10_17485_ijst_2017_v10i7_111220 crossref_primary_10_1002_2211_5463_12588 crossref_primary_10_1016_0922_338X_96_81480_2 crossref_primary_10_1021_jf970707d crossref_primary_10_1007_s00253_004_1781_5 crossref_primary_10_1016_S0167_4838_00_00233_8 crossref_primary_10_1016_j_foodchem_2021_129938 crossref_primary_10_1046_j_1432_1033_2003_03404_x crossref_primary_10_1016_j_carres_2005_07_013 crossref_primary_10_1046_j_1432_1327_2000_01353_x crossref_primary_10_1007_s13205_017_0725_6 crossref_primary_10_1007_s13205_023_03510_5 crossref_primary_10_1016_S1389_1723_00_88740_X crossref_primary_10_3390_futurepharmacol3030035 crossref_primary_10_1016_S0141_0229_01_00461_6 crossref_primary_10_1007_s00253_009_2221_3 |
ContentType | Journal Article |
DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 5PM |
DOI | 10.1128/aem.58.12.4016-4025.1992 |
DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic PubMed Central (Full Participant titles) |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic |
DatabaseTitleList | CrossRef MEDLINE |
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 | Economics Engineering Biology |
EISSN | 1098-5336 |
EndPage | 4025 |
ExternalDocumentID | 10_1128_aem_58_12_4016_4025_1992 1476442 aem_58_12_4016 |
Genre | Journal Article |
GroupedDBID | --- -~X .55 .GJ 0R~ 23M 2WC 39C 3O- 4.4 53G 5GY 5RE 5VS 6J9 85S AAZTW ABOGM ABPPZ ABTAH ACBTR ACGFO ACIWK ACNCT ACPRK ADBBV ADUKH AENEX AFFNX AFRAH AGCDD AGVNZ AI. ALMA_UNASSIGNED_HOLDINGS AOIJS BAWUL BKOMP BTFSW C1A CGR CS3 CUY CVF D0L DIK E.- E3Z EBS ECM EIF EJD F20 F5P GX1 H13 HYE HZ~ H~9 K-O KQ8 L7B MVM NEJ NPM O9- OHT OK1 P2P PQQKQ RHF RHI RNS RPM RSF RXW TAE TAF TN5 TR2 TWZ UCJ UHB VH1 W8F WH7 WHG WOQ X6Y X7M XJT YV5 ZCG ZGI ZXP ZY4 ~02 ~KM AAYXX CITATION 7X8 5PM |
ID | FETCH-LOGICAL-c598t-853636ec04a1300889503de281e9c890a01e7c10131511fe92a947238651e84e3 |
IEDL.DBID | RPM |
ISSN | 0099-2240 |
IngestDate | Tue Sep 17 21:25:29 EDT 2024 Fri Oct 25 04:49:25 EDT 2024 Thu Sep 12 17:25:03 EDT 2024 Sat Sep 28 07:24:55 EDT 2024 Wed May 18 15:26:53 EDT 2016 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 12 |
Language | English |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c598t-853636ec04a1300889503de281e9c890a01e7c10131511fe92a947238651e84e3 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
OpenAccessLink | https://aem.asm.org/content/aem/58/12/4016.full.pdf |
PMID | 1476442 |
PQID | 73423610 |
PQPubID | 23479 |
PageCount | 10 |
ParticipantIDs | proquest_miscellaneous_73423610 pubmed_primary_1476442 pubmedcentral_primary_oai_pubmedcentral_nih_gov_183219 highwire_asm_aem_58_12_4016 crossref_primary_10_1128_aem_58_12_4016_4025_1992 |
PublicationCentury | 1900 |
PublicationDate | 1992-12-01 |
PublicationDateYYYYMMDD | 1992-12-01 |
PublicationDate_xml | – month: 12 year: 1992 text: 1992-12-01 day: 01 |
PublicationDecade | 1990 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States |
PublicationTitle | Applied and Environmental Microbiology |
PublicationTitleAlternate | Appl Environ Microbiol |
PublicationYear | 1992 |
Publisher | American Society for Microbiology |
Publisher_xml | – name: American Society for Microbiology |
References | 2137908 - Nucleic Acids Res. 1990 Jan 11;18(1):199 2972812 - J Gen Microbiol. 1988 Jan;134(1):97-105 3843705 - Anal Biochem. 1985 Oct;150(1):76-85 6678612 - Cell. 1983 May;33(1):53-63 6310323 - Methods Enzymol. 1983;101:20-78 6181373 - Mol Gen Genet. 1982;186(3):339-46 6343825 - Microbiol Rev. 1983 Mar;47(1):1-45 5916452 - Sci Am. 1966 Oct;215(4):55-60 passim 6277855 - J Bacteriol. 1982 Mar;149(3):824-30 6268607 - J Bacteriol. 1981 Sep;147(3):776-86 3530497 - Cell. 1986 Sep 12;46(6):921-8 5420325 - J Mol Biol. 1970 Mar;48(3):443-53 2671995 - Proc Natl Acad Sci U S A. 1989 Sep;86(17):6562-6 3323803 - Methods Enzymol. 1987;153:3-11 6099249 - Cold Spring Harb Symp Quant Biol. 1984;49:401-9 271968 - Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463-7 6609921 - J Biochem. 1984 Mar;95(3):697-702 3127377 - J Bacteriol. 1988 Apr;170(4):1554-9 518863 - Biochemistry. 1979 Dec 11;18(25):5698-703 2524186 - Biochem J. 1989 Apr 1;259(1):145-52 2748349 - Nucleic Acids Res. 1989 Jun 26;17(12):4895 3011735 - J Bacteriol. 1986 Jun;166(3):1118-22 1368519 - Agric Biol Chem. 1990 Jan;54(1):197-201 7338898 - J Mol Biol. 1981 Sep 15;151(2):261-87 13738459 - Biochem Biophys Res Commun. 1961 May 15;5:11-5 344137 - Gene. 1977;2(2):95-113 2482332 - J Gen Microbiol. 1989 Jun;135(6):1521-8 3930658 - J Gen Microbiol. 1985 Jul;131(7):1753-63 5432063 - Nature. 1970 Aug 15;227(5259):680-5 2525902 - Biochem Biophys Res Commun. 1989 Jun 30;161(3):1273-9 7462208 - J Biochem. 1980 Dec;88(6):1895-8 1368573 - Appl Microbiol Biotechnol. 1990 Aug;33(5):542-6 2530917 - Anal Biochem. 1989 Aug 15;181(1):6-11 6387910 - Science. 1984 Nov 2;226(4674):555-7 2993245 - J Bacteriol. 1985 Sep;163(3):824-31 2957361 - J Bacteriol. 1987 Sep;169(9):4399-402 2481445 - Biochem J. 1989 Nov 15;264(1):309-11 1826034 - J Mol Biol. 1991 Feb 20;217(4):737-50 |
References_xml | |
SSID | ssj0004068 |
Score | 1.6711127 |
Snippet | Classifications
Services
AEM
Citing Articles
Google Scholar
PubMed
Related Content
Social Bookmarking
CiteULike
Delicious
Digg
Facebook
Google+
Mendeley
Reddit... Cyclodextrin glucanotransferase (CGTase; EC 2.4.1.19) is produced mainly by Bacillus strains. CGTase from Bacillus macerans IFO3490 produces alpha-cyclodextrin... |
SourceID | pubmedcentral proquest crossref pubmed highwire |
SourceType | Open Access Repository Aggregation Database Index Database Publisher |
StartPage | 4016 |
SubjectTerms | Amino Acid Sequence Bacillus - enzymology Bacillus - genetics Base Sequence Cloning, Molecular DNA, Bacterial - genetics Genes, Bacterial Geobacillus stearothermophilus - enzymology Geobacillus stearothermophilus - genetics Glucosyltransferases - chemistry Glucosyltransferases - genetics Glucosyltransferases - ultrastructure Molecular Sequence Data Molecular Structure Protein Conformation |
Title | Cyclization characteristics of cyclodextrin glucanotransferase are conferred by the NH2-terminal region of the enzyme |
URI | http://aem.asm.org/content/58/12/4016.abstract https://www.ncbi.nlm.nih.gov/pubmed/1476442 https://search.proquest.com/docview/73423610 https://pubmed.ncbi.nlm.nih.gov/PMC183219 |
Volume | 58 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3BattAEB3qQGh6KKnbUCVNuodeZWtX0mp1DKbBtCS00EBui7Qe0YAlB1s-OF-fGUnbxqGnnme1EpoR80b75g3Al5xSXIyOkFuZlmFS8DRAo2WonE5Kk-RKGW4Uvr7R89vk2116NzSFbQZaZePK-0mzrCfN_e-OW_lQu6nniU1_XM84DGU-HcGI4tNX6L4XMtLGK09yuvLsHWWmBdaT1PDfPyoqNFdOKTfrqSM4lElGwEDtJycvGPwv8PmSQ_ksKV0dw9sBTYrL_qnfwStsxnDYz5fcjeG1bzvejOHNM-XB97Cd7dxyaMEUbl-0Wawq4cjMze4tLRdMay-aVdthXFxT3hPFGoXrmgXXuBDlThCOFDdzFQ7kmqXgiQ-0N-3FJmwedzV-gNurr79m83CYwBC6NDdtSLlcxxpdlBR87GVMnkbxApWRmDuTR0UkMXOSNXsIuFWYqyJPeIyZTiWaBOMTOGhWDX4E4SKXLSqsZOZcgooCIXao-BivwlRXJgDpX7196IU2bFegKGPJcTY1VirLjrPsOMuOC-DM-8gWm_rFugA-e7dZ-mb4IKRocLXd2IxlDwk3BnDSO_HvHfs4CEDvefePncW49y0Uo50odx-Tp_974RkcdUTgjijzCQ7a9RbPCe605QWMvv80F12UPwFcuf6C |
link.rule.ids | 230,315,730,783,787,888,27936,27937,53804,53806 |
linkProvider | National Library of Medicine |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3Pb9MwFH6CoWnjwI_CRBgwH7gmjR3HcY6oYiqwVhxWaTcrcV_ERJtObXro_nr8khjWigucn-Mo8me9z_H3vgfwMXcpLkHrmFuZlqEsqBugVjwUVslSy1wITYXCk6kaz-TXm_SmLwrb9LLK2pa3Ub1YRvXtj1Zbebe0Q68TG36fjAiGPB8-hiduu8bSn9F9NWSstPeepITl9TtCDwtcRqmm_3_uWKHo7JRSuZ44hWMuM0cNxH568pbBf6OfhyrKB2np8jnM_Ad1apSf0bYpI3t_4PX4r1_8Ap71PJV96qIv4RHWAzjuOlfuBnDiC5o3A3j6wNPwFWxHO7voizuZ3beDZquKWRemMvrGDWckmC_qVdOyZ1y7jMqKNTLbliGucc7KHXMMlU3HIuxlOwtGvSTc3G4uCmF9v1via5hdfr4ejcO-t0No01w3oWMJKlFoY1nQhZrWeRoncxSaY251Hhcxx8xycgNylLDCXBS5pAZpKuWoJSZncFSvanwDzMY2m1dY8cxaicJBLLEo6IKwwlRVOgDul9TcdRYepj36CG0cIEyqDReGAGEIEIYAEcC5X3tTbJYH4wK48HAwbjfSFUtR42q7MRkZKjpGGsBZB44_b-zwFYDaQ83vONl870ccFlq7727t3_7vgxdwMr6eXJmrL9Nv53Dayo1bOc47OGrWW3zvSFVTfmj30C-dFR9Z |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV09b9swED2kKdKkQz_cBlHTNhy66oOURFFj4dZwP2JkaIB0IiT6hAa1ZMOWB-fXlyeZbWx0ykyKgsBH3Dvx3TuAD7kNcTEay9zKtPSTgroBKsl9YWRSqiQXQlGh8OVEjq-TrzfpzQEoVwvTifZNeRs0szpobn912spFbUKnEwuvLocEQ56Hi2kVPoLH9shG0uXpriIyksr5T1LQchoeocIC6yBV9A_QphaS8qeUSvbECRzxJLP0QOyGKGcb_D8Kuq-kvBeaRs_hp_uoXpHyO1i3ZWDu9vweH_LVL-DZlq-yj_2Ml3CAzQCO-g6WmwEcu8Lm1QCe3vM2fAXr4cbMtkWezOzaQrN5xYwdpnL61k5nJJwvmnnbsWhc2sjKiiUy05UjLnHKyg2zTJVNxsLfyndmjHpK2LXtWjSEzd2mxtdwPfr8Yzj2tz0efJPmqvUtW5CxRBMlBV2sKZWnUTxFoTjmRuVREXHMDCdXIEsNK8xFkSfUKE2mHFWC8SkcNvMGz4CZyGTTCiueGZOgsFCLDQq6KKwwlZXygLtt1YveykN3KZBQ2oJCp0pzoQkUmkChCRQenLv918Wq3pvnwYWDhLankq5aigbn65XOyFjRMlMPTnuA_HtjjzEP5A5y_o6T3ffuiMVDZ_vd7_-bhz54AU-uPo309y-Tb-dw0qmOO1XOWzhsl2t8Z7lVW77vjtEfnQkh2Q |
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=Cyclization+characteristics+of+cyclodextrin+glucanotransferase+are+conferred+by+the+NH2-terminal+region+of+the+enzyme&rft.jtitle=Applied+and+environmental+microbiology&rft.au=Fujiwara%2C+S&rft.au=Kakihara%2C+H&rft.au=Woo%2C+K+B&rft.au=Lejeune%2C+A&rft.date=1992-12-01&rft.issn=0099-2240&rft.eissn=1098-5336&rft.volume=58&rft.issue=12&rft.spage=4016&rft.epage=4025&rft_id=info:doi/10.1128%2Faem.58.12.4016-4025.1992&rft_id=info%3Apmid%2F1476442&rft.externalDBID=PMC183219 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0099-2240&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0099-2240&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0099-2240&client=summon |