Methylamine dehydrogenase from the obligate methylotroph Methylomonas methylovora.
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.
D000445:Aldehyde Oxidoreductases / Q000378:metabolism; D002474:Cell-Free System; D002729:Chloromercuribenzoates / Q000494:pharmacology; D004355:Drug Stability; D005557:Formaldehyde / Q000378:metabolism; D005561:Formates / Q000378:metabolism; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007460:Iodoacetamide / Q000494:pharmacology; D007538:Isoniazid / Q000494:pharmacology; D008744:Methylamines / Q000378:metabolism; D008772:Methylococcaceae / Q000201:enzymology* / Q000378:metabolism; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism
D002729:Chloromercuribenzoates; D005561:Formates; D008744:Methylamines; D005557:Formaldehyde; D000445:Aldehyde Oxidoreductases; D000587:Oxidoreductases Acting on CH-NH Group Donors; D007538:Isoniazid; D007460:Iodoacetamide