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ThYme: a database for thioester-active enzymes

The ThYme (Thioester-active enzYme; http://www.enzyme.cbirc.iastate.edu) database has been constructed to bring together amino acid sequences and 3D (tertiary) structures of all the enzymes constituting the fatty acid synthesis and polyketide synthesis cycles. These enzymes are active on thioester-c...

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Detalles Bibliográficos
Autores principales: Cantu, David C., Chen, Yingfei, Lemons, Matthew L., Reilly, Peter J.
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3013676/
https://www.ncbi.nlm.nih.gov/pubmed/21045059
http://dx.doi.org/10.1093/nar/gkq1072
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author Cantu, David C.
Chen, Yingfei
Lemons, Matthew L.
Reilly, Peter J.
author_facet Cantu, David C.
Chen, Yingfei
Lemons, Matthew L.
Reilly, Peter J.
author_sort Cantu, David C.
collection PubMed
description The ThYme (Thioester-active enzYme; http://www.enzyme.cbirc.iastate.edu) database has been constructed to bring together amino acid sequences and 3D (tertiary) structures of all the enzymes constituting the fatty acid synthesis and polyketide synthesis cycles. These enzymes are active on thioester-containing substrates, specifically those that are parts of the acyl-CoA synthase, acyl-CoA carboxylase, acyl transferase, ketoacyl synthase, ketoacyl reductase, hydroxyacyl dehydratase, enoyl reductase and thioesterase enzyme groups. These groups have been classified into families, members of which are similar in sequences, tertiary structures and catalytic mechanisms, implying common protein ancestry. ThYme is continually updated as sequences and tertiary structures become available.
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spelling pubmed-30136762011-01-03 ThYme: a database for thioester-active enzymes Cantu, David C. Chen, Yingfei Lemons, Matthew L. Reilly, Peter J. Nucleic Acids Res Articles The ThYme (Thioester-active enzYme; http://www.enzyme.cbirc.iastate.edu) database has been constructed to bring together amino acid sequences and 3D (tertiary) structures of all the enzymes constituting the fatty acid synthesis and polyketide synthesis cycles. These enzymes are active on thioester-containing substrates, specifically those that are parts of the acyl-CoA synthase, acyl-CoA carboxylase, acyl transferase, ketoacyl synthase, ketoacyl reductase, hydroxyacyl dehydratase, enoyl reductase and thioesterase enzyme groups. These groups have been classified into families, members of which are similar in sequences, tertiary structures and catalytic mechanisms, implying common protein ancestry. ThYme is continually updated as sequences and tertiary structures become available. Oxford University Press 2011-01 2010-11-02 /pmc/articles/PMC3013676/ /pubmed/21045059 http://dx.doi.org/10.1093/nar/gkq1072 Text en © The Author(s) 2010. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/2.5 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Articles
Cantu, David C.
Chen, Yingfei
Lemons, Matthew L.
Reilly, Peter J.
ThYme: a database for thioester-active enzymes
title ThYme: a database for thioester-active enzymes
title_full ThYme: a database for thioester-active enzymes
title_fullStr ThYme: a database for thioester-active enzymes
title_full_unstemmed ThYme: a database for thioester-active enzymes
title_short ThYme: a database for thioester-active enzymes
title_sort thyme: a database for thioester-active enzymes
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3013676/
https://www.ncbi.nlm.nih.gov/pubmed/21045059
http://dx.doi.org/10.1093/nar/gkq1072
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