THE ESCHERICHIA-COLI CYSG GENE ENCODES S-ADENOSYLMETHIONINE-DEPENDENT UROPORPHYRINOGEN-III METHYLASE

被引：90

作者：

WARREN, MJ ^{[1
]}

ROESSNER, CA ^{[1
]}

SANTANDER, PJ ^{[1
]}

SCOTT, AI ^{[1
]}

机构：

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

来源：

BIOCHEMICAL JOURNAL | 1990年 / 265卷 / 03期

关键词：

D O I：

10.1042/bj2650725

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：

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 13C-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.

引用

页码：725 / 729

页数：5

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