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

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...

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Bibliographic Details
Published inBiochemical journal Vol. 265; no. 3; pp. 725 - 729
Main Authors Warren, M J, Roessner, C A, Santander, P J, Scott, A I
Format Journal Article
LanguageEnglish
Published England 01.02.1990
Subjects
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
Genes, Bacterial
Heme - analogs & derivatives
Heme - biosynthesis
Methyltransferases - genetics
Methyltransferases - metabolism
Plasmids
Spectrophotometry, Ultraviolet
uroporphyrinogen-III methyltransferase
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0264-6021
1470-8728
DOI:10.1042/bj2650725