PMID:19875438

Park H, Lee H, Ro YT, Kim YM

Identification and functional characterization of a gene for the methanol : N,N'-dimethyl-4-nitrosoaniline oxidoreductase from Mycobacterium sp. strain JC1 (DSM 3803).

Microbiology 156:463-71 (2010)
DOI:10.1099/mic.0.034124-0

[ag:ACS29499]

PMID:3514215

Kato N, Yamagami T, Shimao M, Sakazawa C

Formaldehyde dismutase, a novel NAD-binding oxidoreductase from Pseudomonas putida F61.

Eur J Biochem 156:59-64 (1986)
DOI:10.1111/j.1432-1033.1986.tb09548.x

[ag:AAA25818]

Oxidoreductases;
Acting on the aldehyde or oxo group of donors
BRITE hierarchy

formaldehyde:formaldehyde oxidoreductase

2 formaldehyde + H2O = formate + methanol [RN:R00614]

R00614
Reaction

formaldehyde [CPD:C00067];
H2O [CPD:C00001]

The enzyme contains a tightly but noncovalently bound NADP(H) cofactor, as well as Zn2+ and Mg2+. Enzyme-bound NADPH formed by oxidation of formaldehyde to formate is oxidized back to NADP+ by reaction with a second formaldehyde, yielding methanol. The enzyme from the bacterium Mycobacterium sp. DSM 3803 also catalyses the reactions of EC 1.1.99.36, alcohol dehydrogenase (nicotinoprotein) and EC 1.1.99.37, methanol dehydrogenase (nicotinoprotein) [3]. Formaldehyde and acetaldehyde can act as donors; formaldehyde, acetaldehyde and propanal can act as acceptors [1,2].

EC 1.2.98.1 created 1986 as EC 1.2.99.4, modified 2012, transferred 2015 to EC 1.2.98.1

1

Kato, N., Shirakawa, K., Kobayashi, H. and Sakazawa, C.

The dismutation of aldehydes by a bacterial enzyme.

Agric Biol Chem 47:39-46 (1983)

2  [PMID:3514215]

Kato N, Yamagami T, Shimao M, Sakazawa C

Formaldehyde dismutase, a novel NAD-binding oxidoreductase from Pseudomonas putida F61.

Eur J Biochem 156:59-64 (1986)
DOI:10.1111/j.1432-1033.1986.tb09548.x

[ag:AAA25818]

3  [PMID:19875438]

Park H, Lee H, Ro YT, Kim YM

Identification and functional characterization of a gene for the methanol : N,N'-dimethyl-4-nitrosoaniline oxidoreductase from Mycobacterium sp. strain JC1 (DSM 3803).

Microbiology 156:463-71 (2010)
DOI:10.1099/mic.0.034124-0

[ag:ACS29499]