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Discovering new enzymes and metabolic pathways:: Conversion of succinate to propionate by Escherichia coli
被引:123
作者:
Haller, T
Buckel, T
Rétey, J
Gerlt, JA
[1
]
机构:
[1] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA
[2] Univ Karlsruhe, Inst Organ Chem, Lehrstuhl Biochem, D-76128 Karlsruhe, Germany
关键词:
D O I:
10.1021/bi992888d
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
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.
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页码:4622 / 4629
页数:8
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