EC |
1.14.13.238 |
Accepted name: |
dimethylamine monooxygenase |
Reaction: |
dimethylamine + NADPH + H+ + O2 = methylamine + formaldehyde + NADP+ + H2O |
Other name(s): |
dmmABC (gene names) |
Systematic name: |
dimethylamine,NADPH:oxygen oxidoreductase (formaldehyde-forming) |
Comments: |
The enzyme, characterized from several bacterial species, is involved in a pathway for the degradation of methylated amines. It is composed of three subunits, one of which is a ferredoxin, and contains heme iron and an FMN cofactor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Eady, R.R. and Large, P.J. Bacterial oxidation of dimethylamine, a new mono-oxygenase reaction. Biochem. J. 111 (1969) 37P–38P. [PMID: 4389011] |
2. |
Eady, R.R., Jarman, T.R. and Large, P.J. Microbial oxidation of amines. Partial purification of a mixed-function secondary-amine oxidase system from Pseudomonas aminovorans that contains an enzymically active cytochrome-P-420-type haemoprotein. Biochem. J. 125 (1971) 449–459. [PMID: 4401380] |
3. |
Alberta, J.A. and Dawson, J.H. Purification to homogeneity and initial physical characterization of secondary amine monooxygenase. J. Biol. Chem. 262 (1987) 11857–11863. [PMID: 3624236] |
4. |
Lidbury, I., Mausz, M.A., Scanlan, D.J. and Chen, Y. Identification of dimethylamine monooxygenase in marine bacteria reveals a metabolic bottleneck in the methylated amine degradation pathway. ISME J. 11 (2017) 1592–1601. [DOI] [PMID: 28304370] |
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[EC 1.14.13.238 created 2017] |
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