(R)-citramalate synthase in methanogenic archaea

J Bacteriol. 1999 Jan;181(1):331-3. doi: 10.1128/JB.181.1.331-333.1999.

Abstract

The Methanococcus jannaschii gene MJ1392 was cloned, and its protein product was hyperexpressed in Escherichia coli. The resulting protein was purified and shown to catalyze the condensation of pyruvate and acetyl coenzyme A, with the formation of (R)-citramalate. Thus, this gene (cimA) encodes an (R)-citramalate synthase (CimA). This is the first identification of this enzyme, which is likely involved in the biosynthesis of isoleucine.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Acetyltransferases
  • Acyltransferases
  • Base Sequence
  • Cloning, Molecular
  • DNA Primers / genetics
  • Escherichia coli / genetics
  • Gene Expression
  • Genes, Archaeal
  • Kinetics
  • Malates / metabolism*
  • Methanococcus / enzymology*
  • Methanococcus / genetics*
  • Oxo-Acid-Lyases / genetics*
  • Oxo-Acid-Lyases / isolation & purification
  • Oxo-Acid-Lyases / metabolism*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Substrate Specificity

Substances

  • DNA Primers
  • Malates
  • Recombinant Proteins
  • Acyltransferases
  • Acetyltransferases
  • (R)-citramalate synthase
  • Oxo-Acid-Lyases
  • citramalate