The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylase

作者：Martin J. Warren, Charles A. Roessner, Patricio J. Santander, A. Ian Scott · 发表于：Biochemical Journal · 年份：1990 · DOI：10.1042/bj2650725 · 被引用次数：109 · 研究领域：Porphyrin Metabolism and Disorders、Neonatal Health and Biochemistry、Folate and B Vitamins Research

The Escherichia coli cysG gene was successfully subcloned and over-expressed to produce a 52 kDa protein that was purified to homogeneity. This protein was shown to catalyse the S-adenosylmethionine-dependent methylation of uroporphyrinogen III to give a product identified as sirohydrochlorin on the basis of its absorption spectra, incorporation of 14C label from S-adenosyl[Me-14C]methionine and mass and 1H-n.m.r. spectra of its octamethyl ester. Further confirmation of the structure was obtained from a 14C-n.m.r. spectrum of the methyl ester produced by incubation of the methylase with uroporphyrinogen III, derived from [4.6-13C2]porphobilinogen, and S-adenosyl[Me-13C]methionine.