THE ESCHERICHIA-COLI CYSG GENE ENCODES THE MULTIFUNCTIONAL PROTEIN, SIROHEME SYNTHASE

被引：74

作者：

SPENCER, JB ^{[1
]}

STOLOWICH, NJ ^{[1
]}

ROESSNER, CA ^{[1
]}

SCOTT, AI ^{[1
]}

机构：

[1] TEXAS A&M UNIV,CTR BIOL NMR,DEPT CHEM,COLLEGE STN,TX 77843

来源：

FEBS LETTERS | 1993年 / 335卷 / 01期

关键词：

SIROHEME; DEHYDROGENASE; SIROHYDROCHLORIN; FERROCHELATASE; NAD(+);

D O I：

10.1016/0014-5793(93)80438-Z

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：

Previously, the E. coli cysG gene product had been shown to sequentially methylate uro'gen III to produce precorrin-2, hence it was given the trivial name uro'gen III methylase. We now report that in addition to methylase activity, the CysG protein catalyses both the NAD(+) dependent oxidation of precorrin-2 to sirohydrochlorin, but also the insertion of iron into this oxidized intermediate, thereby producing siroheme. Thus CysG is a multifunctional protein solely responsible for siroheme synthesis from uro'gen III in E. coli, and accordingly is renamed siroheme synthase.

引用

页码：57 / 60

页数：4

共 15 条

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