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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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Formato: | Texto |
Lenguaje: | English |
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Oxford University Press
2011
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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. |
format | Text |
id | pubmed-3013676 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
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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