KEGG   ENZYME: 1.14.13.238Help
Entry
EC 1.14.13.238              Enzyme                                 

Name
dimethylamine monooxygenase;
dmmABC (gene names)
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
BRITE hierarchy
Sysname
dimethylamine,NADPH:oxygen oxidoreductase (formaldehyde-forming)
Reaction(IUBMB)
dimethylamine + NADPH + H+ + O2 = methylamine + formaldehyde + NADP+ + H2O [RN:R11805]
Reaction(KEGG)
Substrate
dimethylamine [CPD:C00543];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
methylamine [CPD:C00218];
formaldehyde [CPD:C00067];
NADP+ [CPD:C00006];
H2O [CPD:C00001]
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.
History
EC 1.14.13.238 created 2017
Orthology
K22342  dimethylamine monooxygenase subunit A
K22343  dimethylamine monooxygenase subunit B
K22344  dimethylamine monooxygenase subunit C
Genes
EBT: EBL_c15110 EBL_c15120 EBL_c15130
PMY: Pmen_3453 Pmen_3454 Pmen_3455
PRE: PCA10_14430 PCA10_14440 PCA10_14450 PCA10_19610 PCA10_19620 PCA10_19630
PCQ: PcP3B5_03590 PcP3B5_03600(ophA1_1) PcP3B5_03610 PcP3B5_34290 PcP3B5_34300(ophA1_3) PcP3B5_34310
PPI: YSA_00714 YSA_00715 YSA_00717
PFS: PFLU_2334 PFLU_2335 PFLU_2336
PFE: PSF113_3543 PSF113_3544 PSF113_3545
PVR: PverR02_12530 PverR02_12535 PverR02_12540
PBA: PSEBR_a2223 PSEBR_a2224 PSEBR_a2225
PSV: PVLB_12400 PVLB_12405 PVLB_12410
HPSE: HPF_01260
RGE: RGE_16190
MXA: MXAN_7111
PAMN: pAMV1p0116(dmmA) pAMV1p0117(dmmB) pAMV1p0118(dmmC)
AAY: WYH_03198
ALB: AEB_P1336
BACO: OXB_0420
CAU: Caur_3088
CAG: Cagg_0865
DFC: DFI_07630
RUL: UC8_44060
SLI: Slin_1933
FAE: FAES_2569
 » show all
Taxonomy
Reference
1  [PMID:4389011]
  Authors
Eady RR, Large PJ
  Title
Bacterial oxidation of dimethylamine, a new mono-oxygenase reaction.
  Journal
Biochem J 111:37P-38P (1969)
Reference
2  [PMID:4401380]
  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
3  [PMID:3624236]
  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
4  [PMID:28304370]
  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
ISME J 11:1592-1601 (2017)
DOI:10.1038/ismej.2017.31
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.13.238
IUBMB Enzyme Nomenclature: 1.14.13.238
ExPASy - ENZYME nomenclature database: 1.14.13.238
BRENDA, the Enzyme Database: 1.14.13.238

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