(R)-citramalate synthase in methanogenic archaea.
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.
Howell
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DM
Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061-0308, USA.
Xu
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White
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D000123:Acetyltransferases; D000217:Acyltransferases; D001483:Base Sequence; D003001:Cloning, Molecular; D017931:DNA Primers / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D019766:Genes, Archaeal; D007700:Kinetics; D008293:Malates / Q000378:metabolism*; D017017:Methanococcus / Q000201:enzymology* / Q000235:genetics*; D007652:Oxo-Acid-Lyases / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity
D017931:DNA Primers; D008293:Malates; D011994:Recombinant Proteins; D000217:Acyltransferases; D000123:Acetyltransferases; C116922:(R)-citramalate synthase; D007652:Oxo-Acid-Lyases; C011729:citramalate