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