Spencer J B, Stolowich N J, Roessner C A, Scott A I
Department of Chemistry, Texas A&M University, College Station 77843-3255.
FEBS Lett. 1993 Nov 29;335(1):57-60. doi: 10.1016/0014-5793(93)80438-z.
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.
此前,已证明大肠杆菌cysG基因产物可将尿卟啉原III依次甲基化以生成预钴胺素-2,因此它被赋予了俗名尿卟啉原III甲基转移酶。我们现在报告,除了甲基转移酶活性外,CysG蛋白还催化预钴胺素-2依赖NAD+氧化为硫氢卟啉,并且催化铁插入这种氧化中间体,从而生成 siro 血红素。因此,CysG是一种多功能蛋白,仅负责大肠杆菌中由尿卟啉原III合成siro血红素,因此被重新命名为siro血红素合酶。