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New Insights about Enzyme Evolution from Large Scale Studies of Sequence and Structure Relationships
Understanding how enzymes have evolved offers clues about their structure-function relationships and mechanisms. Here, we describe evolution of functionally diverse enzyme superfamilies, each representing a large set of sequences that evolved from a common ancestor and that retain conserved features...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2014
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4215206/ https://www.ncbi.nlm.nih.gov/pubmed/25210038 http://dx.doi.org/10.1074/jbc.R114.569350 |
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author | Brown, Shoshana D. Babbitt, Patricia C. |
author_facet | Brown, Shoshana D. Babbitt, Patricia C. |
author_sort | Brown, Shoshana D. |
collection | PubMed |
description | Understanding how enzymes have evolved offers clues about their structure-function relationships and mechanisms. Here, we describe evolution of functionally diverse enzyme superfamilies, each representing a large set of sequences that evolved from a common ancestor and that retain conserved features of their structures and active sites. Using several examples, we describe the different structural strategies nature has used to evolve new reaction and substrate specificities in each unique superfamily. The results provide insight about enzyme evolution that is not easily obtained from studies of one or only a few enzymes. |
format | Online Article Text |
id | pubmed-4215206 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-42152062014-11-05 New Insights about Enzyme Evolution from Large Scale Studies of Sequence and Structure Relationships Brown, Shoshana D. Babbitt, Patricia C. J Biol Chem Minireviews Understanding how enzymes have evolved offers clues about their structure-function relationships and mechanisms. Here, we describe evolution of functionally diverse enzyme superfamilies, each representing a large set of sequences that evolved from a common ancestor and that retain conserved features of their structures and active sites. Using several examples, we describe the different structural strategies nature has used to evolve new reaction and substrate specificities in each unique superfamily. The results provide insight about enzyme evolution that is not easily obtained from studies of one or only a few enzymes. American Society for Biochemistry and Molecular Biology 2014-10-31 2014-09-10 /pmc/articles/PMC4215206/ /pubmed/25210038 http://dx.doi.org/10.1074/jbc.R114.569350 Text en © 2014 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version full access. Creative Commons Attribution Unported License (http://creativecommons.org/licenses/by/3.0/) applies to Author Choice Articles |
spellingShingle | Minireviews Brown, Shoshana D. Babbitt, Patricia C. New Insights about Enzyme Evolution from Large Scale Studies of Sequence and Structure Relationships |
title | New Insights about Enzyme Evolution from Large Scale Studies of Sequence and Structure Relationships |
title_full | New Insights about Enzyme Evolution from Large Scale Studies of Sequence and Structure Relationships |
title_fullStr | New Insights about Enzyme Evolution from Large Scale Studies of Sequence and Structure Relationships |
title_full_unstemmed | New Insights about Enzyme Evolution from Large Scale Studies of Sequence and Structure Relationships |
title_short | New Insights about Enzyme Evolution from Large Scale Studies of Sequence and Structure Relationships |
title_sort | new insights about enzyme evolution from large scale studies of sequence and structure relationships |
topic | Minireviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4215206/ https://www.ncbi.nlm.nih.gov/pubmed/25210038 http://dx.doi.org/10.1074/jbc.R114.569350 |
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