Methylamine dehydrogenase from the obligate methylotroph Methylomonas methylovora

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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 dehydrogenese was purified 21-fold. The enzyme had optimum activity at pH 7.5 and was stable at 60 °C for 5 min. The enzyme activity was inhibited by parachloromercuric benzoate, isonicotinic acid hydrazide, mercuric chloride, and sodium borate.