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J Biol Chem. 2014 Oct 31;289(44):30221-8. doi: 10.1074/jbc.R114.569350. Epub 2014 Sep 10.

New insights about enzyme evolution from large scale studies of sequence and structure relationships.

Author information

1
From the Departments of Bioengineering and Therapeutic Sciences and.
2
From the Departments of Bioengineering and Therapeutic Sciences and Pharmaceutical Chemistry, School of Pharmacy, and the California Institute for Quantitative Biosciences, University of California, San Francisco, California 94158-2330 babbitt@cgl.ucsf.edu.

Abstract

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.

KEYWORDS:

Computational Biology; Enzyme; Enzyme Evolution; Enzyme Structure-Function Relationships; Enzyme Superfamily; Molecular Evolution; Multifunctional Enzyme; Networks; Protein Evolution

PMID:
25210038
PMCID:
PMC4215206
DOI:
10.1074/jbc.R114.569350
[Indexed for MEDLINE]
Free PMC Article

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