Contains Zn2+ and Mg2+. Nicotinoprotein methanol dehydrogenases have a tightly bound NADP+/NADPH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro. The enzyme has been detected in several Gram-positive methylotrophic bacteria, including Amycolatopsis methanolica, Rhodococcus rhodochrous and Rhodococcus erythropolis [1-3]. These enzymes are decameric, and possess a 5-fold symmetry . Some of the enzymes can also dismutate formaldehyde to methanol and formate .
The enzyme appears in viruses and cellular organisms
the low coenzyme NAD-dependent activity of MDH with C1-C4 primary alcohols is strongly stimulated by Bacillus methanolicus protein ACT, in presence of NAD(H) cofactor and Mg2+-ions. MDH activation by ACT involves hydrolytic removal of the nicotinamide mononucleotide NMN(H) moiety of the NAD(H) cofactor of MDH, changing its Ping-Pong type of reaction mechanism into a ternary complex reaction mechanism
the low coenzyme NAD-dependent activity of MDH with C1-C4 primary alcohols is strongly stimulated by Bacillus methanolicus protein ACT, in presence of NAD(H) cofactor and Mg2+-ions. MDH activation by ACT involves hydrolytic removal of the nicotinamide mononucleotide NMN(H) moiety of the NAD(H) cofactor of MDH, changing its Ping-Pong type of reaction mechanism into a ternary complex reaction mechanism
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SYSTEMATIC NAME
IUBMB Comments
methanol:acceptor oxidoreductase
Contains Zn2+ and Mg2+. Nicotinoprotein methanol dehydrogenases have a tightly bound NADP+/NADPH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro. The enzyme has been detected in several Gram-positive methylotrophic bacteria, including Amycolatopsis methanolica, Rhodococcus rhodochrous and Rhodococcus erythropolis [1-3]. These enzymes are decameric, and possess a 5-fold symmetry [4]. Some of the enzymes can also dismutate formaldehyde to methanol and formate [5].
the low coenzyme NAD-dependent activity of MDH with C1-C4 primary alcohols is strongly stimulated by Bacillus methanolicus protein ACT, in presence of NAD(H) cofactor and Mg2+-ions. In the deduced ACT amino acid sequence, the highly conserved amino acid sequence motif typical of Nudix hydrolase proteins is present. MDH activation by ACT involves hydrolytic removal of the nicotinamide mononucleotide NMN(H) moiety of the NAD(H) cofactor of MDH, changing its Ping-Pong type of reaction mechanism into a ternary complex reaction mechanism
Km value of wild-type for NAD+ 0.04 mM, for NADH 0.01 mM, in absence of Mg2+, and for NAD+ 0.03 mM, for NADH 0.011 mM, in presence of Mg2+, of respectively
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of quaternary protein structure by electron microscopy and image processing. Enzyme is a decameric protein displaying fivefold symmetry and possessing a tightly but noncovalently bound NADPH cofactor
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription of methanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase is upregulated in cells growing on methanol compared with cells growing on glucose
transcription of methanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase is upregulated in cells growing on methanol compared with cells growing on glucose
transcription of methanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase is upregulated in cells growing on methanol compared with cells growing on glucose
transcription of methanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase is upregulated in cells growing on methanol compared with cells growing on glucose
Molecular, biochemical, and functional characterization of a Nudix hydrolase protein that stimulates the activity of a nicotinoprotein alcohol dehydrogenase
Identification and functional characterization of a gene for the methanol: N,N'-dimethyl-4-nitrosoaniline oxidoreductase from Mycobacterium sp. strain JC1 (DSM 3803)
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