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Curr Opin Struct Biol. 2011 Jun;21(3):391-7. doi: 10.1016/j.sbi.2011.03.007. Epub 2011 Apr 1.

Topological variation in the evolution of new reactions in functionally diverse enzyme superfamilies.

Author information

1
Department of Pharmaceutical Chemistry, University of California, 600 16th Street, San Francisco, CA 94158-2517, USA.

Abstract

In functionally diverse enzyme superfamilies (SFs), conserved structural and active site features reflect catalytic capabilities 'hard-wired' in each SF architecture. Overlaid on this foundation, evolutionary changes in active site machinery, structural topology and other aspects of structural organization and interactions support the emergence of new reactions, mechanisms, and substrate specificity. This review connects topological with functional variation in each of the haloalkanoic acid dehalogenase (HAD) and vicinal oxygen chelate fold (VOC) SFs and a set of redox-active thioredoxin (Trx)-fold SFs to illustrate a few of the varied themes nature has used to evolve new functions from a limited set of structural scaffolds.

PMID:
21458983
PMCID:
PMC3551608
DOI:
10.1016/j.sbi.2011.03.007
[Indexed for MEDLINE]
Free PMC Article

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