Methylamine dehydrogenase from the obligate methylotroph Methylomonas methylovora

Can J Microbiol. 1977 Apr;23(4):402-6. doi: 10.1139/m77-059.

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.

MeSH terms

  • Aldehyde Oxidoreductases / metabolism
  • Cell-Free System
  • Chloromercuribenzoates / pharmacology
  • Drug Stability
  • Formaldehyde / metabolism
  • Formates / metabolism
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Iodoacetamide / pharmacology
  • Isoniazid / pharmacology
  • Methylamines / metabolism
  • Methylococcaceae / enzymology*
  • Methylococcaceae / metabolism
  • Oxidoreductases Acting on CH-NH Group Donors* / antagonists & inhibitors
  • Oxidoreductases Acting on CH-NH Group Donors* / isolation & purification
  • Oxidoreductases Acting on CH-NH Group Donors* / metabolism

Substances

  • Chloromercuribenzoates
  • Formates
  • Methylamines
  • Formaldehyde
  • Aldehyde Oxidoreductases
  • Oxidoreductases Acting on CH-NH Group Donors
  • Isoniazid
  • Iodoacetamide