The enolase superfamily: Different reactions catalyzed by similar active sites

John Alan Gerlt, P. C. Babbitt

Research output: Contribution to journalArticle

Abstract

The members of the enolase superfarnily of enzymes are related by their ability to catalyze abstraction of an a-proton from a carboxylic acid substrate to generate stabilized enolate/enolic intermediates. These intermediates partition to the diverse products by different mechanisms, including racemization/epirnerization, -elimination of water or ammonia, and cycloisomerizatiort. I.ike all members of their fold class, the rf/tt barrels, the active sites are located in a depression defined by the ('-terminal ends of the eight 3she<'ts: the functional groups involved in catalysis are located at the ends of separate J sheets. This location of functional groups allows chemistry to be (re (directed from a variety of geometric orientations relative to the bound substrates, thereby allowing the evolution of new catalytic functions while retaining the ability to generate enolate/enoHc intermediates. Details of the dependence of function on structure are being characterized in several members of the enolase superfamily, including mandelate racemase. galattnnate and glucarate dehydraiases, N-acylamtnoacid racemase, and carboxyphosphonoenolpynivate synithase.

Original languageEnglish (US)
JournalFASEB Journal
Volume11
Issue number9
StatePublished - 1997

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

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