Methylamine dehydrogenase from the obligate methylotroph Methylomonas methylovora.

Abstract:

:An obligate methyltroph Methylomonas methylovora oxidized methylamine, formaldehyde, and formate. Enzymes oxidizing these substrates were detected in a cell-free system. Phenazine methosulfate-linked methylamine dehydrogenase was purified 21-fold. The enzyme had optimum activity at pH 7.5 and was stable at 60 degrees C for 5 min. The enzyme activity was inhibited by parachloromercuric benzoate, isonicotinic acid hydrazide, mercuric chloride, and sodium borate.

journal_name

Can J Microbiol

authors

Mehta RJ

doi

10.1139/m77-059

subject

Has Abstract

pub_date

1977-04-01 00:00:00

pages

402-6

issue

4

eissn

0008-4166

issn

1480-3275

journal_volume

23

pub_type

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