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

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. (The full text of this publication is not available from this repository)

The full text of this publication is not available from this repository. (Contact us about this Publication)

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
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: 16 Apr 2014 10:52
Resource URI: http://kar.kent.ac.uk/id/eprint/11123 (The current URI for this page, for reference purposes)
  • Depositors only (login required):