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. | |
【 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
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO201912020298775ZK.pdf | 506KB | download |