PMID:2407234
| Citation |
Warren, MJ, Roessner, CA, Santander, PJ and Scott, AI (1990) The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylase. Biochem. J. 265:725-9 |
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| Abstract |
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. |
| Links | |
| Keywords |
Bacterial Proteins/biosynthesis; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Catalysis; Chemical Phenomena; Chemistry; Chromatography, High Pressure Liquid; Electrophoresis, Polyacrylamide Gel; Escherichia coli/genetics; Gene Expression; Genes, Bacterial; Heme/analogs & derivatives; Heme/biosynthesis; Methyltransferases/genetics; Methyltransferases/metabolism; Plasmids; Spectrophotometry, Ultraviolet |
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