UNSPECIFIED (1996) Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme. MICROBIOLOGY-UK, 142 (Part 2). pp. 251-260. ISSN 1350-0872

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Abstract

A novel methylotroph, strain M2, capable of utilizing methanesulfonic acid (MSA) as a sole source of carbon and energy was the subject of these investigations, The initial step in the biodegradative pathway of MSA in strain M2 involved an inducible NADH-specific monooxygenase enzyme (MSAMO). Partial purification of MSAMO from cell-free extracts by ion-exchange chromatography led to the loss of MSAMO activity. Activity was restored by the mixing of three distinct protein fractions designated A, B and C. The reconstituted enzyme had a narrow substrate specificity relative to crude cell-free extracts. Addition of FAD and ferrous ions to the reconstituted enzyme complex resulted in a fivefold increase in enzyme activity, suggesting the loss of FAD and ferrous ion from the multicomponent enzyme on purification. Analysis of mutants of strain M2 defective in the metabolism of C-1 compounds indicated that methanol was not an intermediate in the degradative pathway of MSA and also confirmed the involvement of a multicomponent enzyme in the degradation of MSA by methylotroph strain M2.

Item Type:	Journal Article
Subjects:	Q Science > QR Microbiology
Journal or Publication Title:	MICROBIOLOGY-UK
Publisher:	SOC GENERAL MICROBIOLOGY
ISSN:	1350-0872
Date:	February 1996
Volume:	142
Number:	Part 2
Number of Pages:	10
Page Range:	pp. 251-260
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/19044

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