Divergent evolution in enolase superfamily: Strategies for assigning functions

John A. Gerlt, Patricia C. Babbitt, Matthew P. Jacobson, Steven C. Almo

Research output: Contribution to journalArticle

88 Citations (Scopus)

Abstract

Nature's strategies for evolving catalytic functions can be deciphered from the information contained in the rapidly expanding protein sequence databases. However, the functions of many proteins in the protein sequence and structure databases are either uncertain (too divergent to assign function based on homology) or unknown (no homologs), thereby limiting the utility of the databases. The mechanistically diverse enolase superfamily is a paradigm for understanding the structural bases for evolution of enzymatic function. We describe strategies for assigning functions to members of the enolase superfamily that should be applicable to other superfamilies.

Original languageEnglish (US)
Pages (from-to)29-34
Number of pages6
JournalJournal of Biological Chemistry
Volume287
Issue number1
DOIs
StatePublished - Jan 2 2012

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Protein Databases
Phosphopyruvate Hydratase
Proteins
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ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Divergent evolution in enolase superfamily : Strategies for assigning functions. / Gerlt, John A.; Babbitt, Patricia C.; Jacobson, Matthew P.; Almo, Steven C.

In: Journal of Biological Chemistry, Vol. 287, No. 1, 02.01.2012, p. 29-34.

Research output: Contribution to journalArticle

Gerlt, John A. ; Babbitt, Patricia C. ; Jacobson, Matthew P. ; Almo, Steven C. / Divergent evolution in enolase superfamily : Strategies for assigning functions. In: Journal of Biological Chemistry. 2012 ; Vol. 287, No. 1. pp. 29-34.
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