Entry |
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Name |
dimethylamine monooxygenase;
dmmABC (gene names)
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Class |
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
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Sysname |
dimethylamine,NADPH:oxygen oxidoreductase (formaldehyde-forming)
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Reaction(IUBMB) |
dimethylamine + NADPH + H+ + O2 = methylamine + formaldehyde + NADP+ + H2O [RN: R11805]
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Reaction(KEGG) |
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Substrate |
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Product |
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Comment |
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.
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History |
EC 1.14.13.238 created 2017
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Orthology |
K22342 | dimethylamine monooxygenase subunit A |
K22343 | dimethylamine monooxygenase subunit B |
K22344 | dimethylamine monooxygenase subunit C |
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Genes |
» show all
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Reference |
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Authors |
Eady RR, Large PJ |
Title |
Bacterial oxidation of dimethylamine, a new mono-oxygenase reaction. |
Journal |
Biochem J 111:37P-38P (1969) |
Reference |
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Authors |
Eady RR, Jarman TR, Large PJ |
Title |
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. |
Journal |
Biochem J 125:449-59 (1971) |
Reference |
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Authors |
Alberta JA, Dawson JH |
Title |
Purification to homogeneity and initial physical characterization of secondary amine monooxygenase. |
Journal |
J Biol Chem 262:11857-63 (1987) |
Reference |
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Authors |
Lidbury I, Mausz MA, Scanlan DJ, Chen Y |
Title |
Identification of dimethylamine monooxygenase in marine bacteria reveals a metabolic bottleneck in the methylated amine degradation pathway. |
Journal |
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Sequence |
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Other DBs |
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