PMID: 4314Mar 16, 1976

Purification and properties of a methanol-oxidizing enzyme in Pseudomonas C

European Journal of Biochemistry
I Goldberg

Abstract

A methanol-oxidizing enzyme has been purified from Pseudomonas C, grown on methanol as a sole source for carbon and energy. The purification procedure involved ammonium sulphate precipitation, ion-exchange chromatography and gel filtration and resulted in a yield of 35.4%. Enzyme activity can be coupled to phenazine methosulfate and requires the presence of ammonium ions in the assay mixtures. The enzymes possesses a broad specificity for primary alcohols. Formaldehyde is also oxidized by the purified enzyme. The Km value for methanol is 15 muM. The optimum pH for the oxidation of both methanol and formaldehyde is about 10.4. The enzyme has a molecular weight of about 128000 and consists of two subunits each having a molecular weight of 60000.

References

Nov 1, 1975·Journal of Bacteriology·I Goldberg, R I Mateles
Feb 1, 1972·Journal of Bacteriology·J S DahlD S Hoare
Apr 1, 1973·Journal of Bacteriology·B Stieglitz, R I Mateles
Jan 1, 1970·Annual Review of Microbiology·D W RibbonsA M Wadzinski
Sep 1, 1965·The Biochemical Journal·C Anthony, L J Zatman
Oct 15, 1966·Nature·D CavalliniS Dupré

Citations

Oct 4, 1978·Archives of Microbiology·C W Bamforth, J R Quayle
May 1, 1989·Antonie van Leeuwenhoek·J FrankJ A Duine
Jan 1, 1978·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·E Cardemil
Jul 1, 1979·The British Journal of Oral Surgery·J P Rood, J Murgatroyd
Jan 1, 1978·Zeitschrift für allgemeine Mikrobiologie·W Babel, G Mothes

Related Concepts

Alcohol Oxidoreductases
Sodium Methoxide
Drug Stability
Hydrogen-Ion Concentration
Pseudomonas
Spectrophotometry, Ultraviolet
Structure-Activity Relationship

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