| EC |
1.2.98.1 |
| Accepted name: |
formaldehyde dismutase |
| Reaction: |
2 formaldehyde + H2O = formate + methanol |
| Other name(s): |
aldehyde dismutase; cannizzanase; nicotinoprotein aldehyde dismutase |
| Systematic name: |
formaldehyde:formaldehyde oxidoreductase |
| Comments: |
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]. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 85204-94-0 |
| References: |
| 1. |
Kato, N., Shirakawa, K., Kobayashi, H. and Sakazawa, C. The dismutation of aldehydes by a bacterial enzyme. Agric. Biol. Chem. 47 (1983) 39–46. |
| 2. |
Kato, N., Yamagami, T., Shimao, M. and Sakazawa, C. Formaldehyde dismutase, a novel NAD-binding oxidoreductase from Pseudomonas putida F61. Eur. J. Biochem. 156 (1986) 59–64. [DOI] [PMID: 3514215] |
| 3. |
Park, H., Lee, H., Ro, Y.T. and Kim, Y.M. 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 (2010) 463–471. [DOI] [PMID: 19875438] |
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| [EC 1.2.98.1 created 1986 as EC 1.2.99.4, modified 2012, transferred 2015 to EC 1.2.98.1] |
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