Discovering new enzymes and metabolic pathways: Conversion of succinate to propionate by Escherichia coli

Toomas Haller, Thomas Buckel, János Rétey, John Alan Gerlt

Research output: Contribution to journalArticle

Abstract

The Escherichia coli genome encodes seven paralogues of the crotonase (enoyl CoA hydratase) superfamily. Four of these have unknown or uncertain functions; their existence was unknown prior to the completion of the E. coli genome sequencing project. The gene encoding one of these, YgfG, is located in a four-gene operon that encodes homologues of methylmalonyl CoA mutases (Sbm) and acyl CoA transferases (YgfH) as well as a putative protein kinase (YgfD/ArgK). We have determined that YgfG is methylmalonyl CoA decarboxylase, YgfH is propionyl CoA:succinate CoA transferase, and Sbm is methylmalonyl CoA mutase. These reactions are sufficient to form a metabolic cycle by which E. coli can catalyze the decarboxylation of succinate to propionate, although the metabolic context of this cycle is unknown. The identification of YgfG as methylmalonyl CoA decarboxylase expands the range of reactions catalyzed by members of the crotonase superfamily.

Original languageEnglish (US)
Pages (from-to)4622-4629
Number of pages8
JournalBiochemistry
Volume39
Issue number16
DOIs
StatePublished - Apr 25 2000

ASJC Scopus subject areas

  • Biochemistry

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