Warren, M.J. and Roessner, C.A. and Santander, P.J. and Scott, A.I. (1990) The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylase. BIOCHEMICAL JOURNAL, 265 (3). pp. 725-9. ISSN 0264-6021 .
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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.
| Item Type: | Article |
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| Additional information: | |
| Uncontrolled keywords: | Bacterial Proteins/biosynthesis/genetics/isolation & purification Catalysis Chemistry Chromatography, High Pressure Liquid Electrophoresis, Polyacrylamide Gel Escherichia coli/*genetics Gene Expression *Genes, Bacterial Heme/analogs & derivatives/biosynthesis Methyltransferases/*genetics/metabolism Plasmids Spectrophotometry, Ultraviolet |
| Subjects: | Q Science |
| Divisions: | Faculties > Science Technology and Medical Studies > School of Biosciences |
| Depositing User: | Martin Warren |
| Date Deposited: | 21 Oct 2009 08:36 |
| Last Modified: | 14 Jan 2010 14:42 |
| Resource URI: | http://kar.kent.ac.uk/id/eprint/11123 (The current URI for this page, for reference purposes) |
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