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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...

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Detalles Bibliográficos
Autores principales: Brown, Shoshana D., Babbitt, Patricia C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2014
Materias:
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.
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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.
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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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