期刊论文详细信息
FEBS Letters
The Escherichia coli cysG gene encodes the multifunctional protein, siroheme synthase
Spencer, Jonathan B.1  Scott, A.Ian1  Roessner, Charles A.1  Stolowich, Neal J.1 
[1] Center for Biological NMR, Department of Chemistry, Texas A&M University, College Station, TX 77843-3255, USA
关键词: Siroheme;    Dehydrogenase;    Sirohydrochlorin;    Ferrochelatase;    NAD+;   
DOI  :  10.1016/0014-5793(93)80438-Z
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 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.

【 授权许可】

Unknown   

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