Format

Send to

Choose Destination
Biochemistry. 2000 Apr 25;39(16):4622-9.

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

Author information

1
Department of Biochemistry, University of Illinois, Urbana, Illinois 61801, USA.

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.

PMID:
10769117
DOI:
10.1021/bi992888d
[Indexed for MEDLINE]

Publication types, MeSH terms, Substances, Secondary source ID, Grant support

Supplemental Content

Full text links

Icon for American Chemical Society
Loading ...
Support Center