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Updated: Jul 28, 2026

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Methanol Independent Expression by Pichia Pastoris Employing De-repression Technologies
Published on: January 23, 2019
An improved assay for bacterial methane mono-oxygenase: some properties of the enzyme from Methylomonas methanica
The Biochemical Journal
|November 1, 1975
Abstract:
Extracts of Methylomonas methanica catalyse the O2-and NAD(P)H-dependent disappearance of bromomethane. The activity is unstable at 2 degrees C but is stable at --70 degrees C for several weeks. Bromomethane mono-oxygenase is particulate and is inhibited by metal-binding reagents, by compounds SKF 525A and Lilly 53325, by some metal ions and by acetylene. Evidence is presented that indicates that bromomethane mono-oxygenase is the enzyme responsible for methane oxidation in vivo.
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