Literature DB >> 21458983

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

Elaine C Meng1, Patricia C Babbitt.   

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.
Copyright © 2011 Elsevier Ltd. All rights reserved.

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Year:  2011        PMID： 21458983      PMCID： PMC3551608          DOI： 10.1016/j.sbi.2011.03.007

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN： 0959-440X            Impact factor:   6.809


  42 in total

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4.  Evolutionary genomics of the HAD superfamily: understanding the structural adaptations and catalytic diversity in a superfamily of phosphoesterases and allied enzymes.

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Journal:  J Mol Biol       Date:  2006-07-07       Impact factor: 5.469

5.  The origami of thioredoxin-like folds.

Authors:  Jonathan L Pan; James C A Bardwell
Journal:  Protein Sci       Date:  2006-10       Impact factor: 6.725

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Review 7.  Divergence and convergence in enzyme evolution.

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8.  Large-scale determination of sequence, structure, and function relationships in cytosolic glutathione transferases across the biosphere.

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Review 9.  The evolution of enzyme function in the isomerases.

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