Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme
UNSPECIFIED. (1996) Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme. MICROBIOLOGY-UK, 142 (Part 2). pp. 251-260. ISSN 1350-0872Full text not available from this repository.
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|
|Official Date:||February 1996|
|Number of Pages:||10|
|Page Range:||pp. 251-260|
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