| Thioesterases: a new perspective based on their primary and tertiary structures. | |
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MedLine Citation:
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PMID: 20506386 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Thioesterases (TEs) are classified into EC 3.1.2.1 through EC 3.1.2.27 based on their activities on different substrates, with many remaining unclassified (EC 3.1.2.-). Analysis of primary and tertiary structures of known TEs casts a new light on this enzyme group. We used strong primary sequence conservation based on experimentally proved proteins as the main criterion, followed by verification with tertiary structure superpositions, mechanisms, and catalytic residue positions, to accurately define TE families. At present, TEs fall into 23 families almost completely unrelated to each other by primary structure. It is assumed that all members of the same family have essentially the same tertiary structure; however, TEs in different families can have markedly different folds and mechanisms. Conversely, the latter sometimes have very similar tertiary structures and catalytic mechanisms despite being only slightly or not at all related by primary structure, indicating that they have common distant ancestors and can be grouped into clans. At present, four clans encompass 12 TE families. The new constantly updated ThYme (Thioester-active enzYmes) database contains TE primary and tertiary structures, classified into families and clans that are different from those currently found in the literature or in other databases. We review all types of TEs, including those cleaving CoA, ACP, glutathione, and other protein molecules, and we discuss their structures, functions, and mechanisms. |
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Authors:
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David C Cantu; Yingfei Chen; Peter J Reilly |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Review |
Journal Detail:
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Title: Protein science : a publication of the Protein Society Volume: 19 ISSN: 1469-896X ISO Abbreviation: Protein Sci. Publication Date: 2010 Jul |
Date Detail:
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Created Date: 2010-06-29 Completed Date: 2010-09-29 Revised Date: 2011-08-01 |
Medline Journal Info:
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Nlm Unique ID: 9211750 Medline TA: Protein Sci Country: United States |
Other Details:
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Languages: eng Pagination: 1281-95 Citation Subset: IM |
Affiliation:
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Department of Chemical and Biological Engineering, Iowa State University, Ames, Iowa 50011, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Databases, Protein Humans Protein Structure, Tertiary Sequence Homology, Amino Acid Thiolester Hydrolases / chemistry*, metabolism |
| Chemical | |
Reg. No./Substance:
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EC 3.1.2.-/Thiolester Hydrolases |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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