KEGG   ENZYME: 1.4.9.1Help
Entry
EC 1.4.9.1                  Enzyme                                 

Name
methylamine dehydrogenase (amicyanin);
amine dehydrogenase;
primary-amine dehydrogenase;
amine: (acceptor) oxidoreductase (deaminating);
primary-amine:(acceptor) oxidoreductase (deaminating)
Class
Oxidoreductases;
Acting on the CH-NH2 group of donors;
With a copper protein as acceptor
BRITE hierarchy
Sysname
methylamine:amicyanin oxidoreductase (deaminating)
Reaction(IUBMB)
methylamine + H2O + 2 amicyanin = formaldehyde + NH3 + 2 reduced amicyanin [RN:R00606]
Reaction(KEGG)
Substrate
methylamine [CPD:C00218];
H2O [CPD:C00001];
amicyanin [CPD:C19671]
Product
formaldehyde [CPD:C00067];
NH3 [CPD:C00014];
reduced amicyanin [CPD:C19672]
Comment
Contains tryptophan tryptophylquinone (TTQ) cofactor. The enzyme oxidizes aliphatic monoamines and diamines, histamine and ethanolamine, but not secondary and tertiary amines, quaternary ammonium salts or aromatic amines.
History
EC 1.4.9.1 created 1978 as EC 1.4.99.3, modified 1986, transferred 2011 to EC 1.4.98.1, transferred 2011 to EC 1.4.9.1
Pathway
ec00680  Methane metabolism
ec01120  Microbial metabolism in diverse environments
Orthology
K08685  quinohemoprotein amine dehydrogenase
K15228  methylamine dehydrogenase light chain
K15229  methylamine dehydrogenase heavy chain
Genes
VFU: vfu_A02015 vfu_A02018
VFL: AL536_13995 AL536_14010
PMK: MDS_2876 MDS_2877 MDS_4213 MDS_4216
PRE: PCA10_23420(mauB) PCA10_23450(mauA) PCA10_32510(peaA) PCA10_34250(mauB) PCA10_34280(mauA)
PCQ: PcP3B5_29870 PcP3B5_30140(aauA) PcP3B5_30170(aauB)
PPU: PP_5602(peaA)
PPF: Pput_2307
PPG: PputGB1_2221 PputGB1_2224 PputGB1_2475
PPW: PputW619_2945
PPT: PPS_2940
PPI: YSA_11298
PPX: T1E_1613
PPUH: B479_14560
PPUT: L483_18160
PPUN: PP4_23960(peaA)
PPUD: DW66_3200
PMON: X969_14050
PMOT: X970_13695
PFL: PFL_4120(peaA)
PPRO: PPC_4221(peaA)
PMAN: OU5_1439
PKC: PKB_2656(mauA) PKB_2659(mauB) PKB_2912
PSEM: TO66_21570
PSOS: POS17_4220(peaA)
PSIL: PMA3_20245
PSE: NH8B_2195
BCEN: DM39_4450(peaA)
BMK: DM80_4965 DM80_4968(aauA)
BMUL: NP80_4958(aauA) NP80_4961
BCED: DM42_5686 DM42_5689(aauA)
BDL: AK34_3489 AK34_3492(aauA)
AMIM: MIM_c29740(mauA) MIM_c29770(mauB)
MPT: Mpe_A2653
EBA: ebA2235(qhpA) ebA5178(qhpA)
AZO: azo1239(qhpA) azo2257(mauA) azo2260(maub)
AZA: AZKH_3023(qhpA)
TCL: Tchl_2123
ABU: Abu_0465
ABT: ABED_0440
ARC: ABLL_0607
DTO: TOL2_C06430(qhpA)
MEA: Mex_1p2770(mauB) Mex_1p2773(mauA)
METD: C0214_27025(mauA) C0214_27040(mauB)
FIL: BN1229_v1_3765(mauB) BN1229_v1_3768(mauA)
FIY: BN1229_v1_3755(mauB) BN1229_v1_3758(mauA)
PYE: A6J80_01745(peaA) A6J80_21995(mauB) A6J80_22010(mauA)
PZH: CX676_03775(peaA)
PARO: CUV01_13130(peaA)
RHC: RGUI_4107
LABR: CHH27_09745(peaA)
THAS: C6Y53_00400(peaA)
SPHR: BSY17_2364(peaA) BSY17_2810(mauA) BSY17_2813
GDI: GDI0271(mauB) GDI0273(mauA) GDI1806(mauB) GDI1807(mauA)
APK: APA386B_1936(mauB) APA386B_1939(mauA)
ASZ: ASN_2153(mauB) ASN_2156(mauA)
MAGX: XM1_2531
BACO: OXB_3506
RER: RER_53630
REY: O5Y_25460
REQ: REQ_44990(mauA)
RHS: A3Q41_02066(mauA)
RRT: 4535765_00133(mauA)
 » show all
Taxonomy
Reference
1  [PMID:6246962]
  Authors
de Beer R, Duine JA, Frank J, Large PJ.
  Title
The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1: evidence for a quinone structure.
  Journal
Biochim Biophys Acta 622:370-4 (1980)
DOI:10.1016/0005-2795(80)90050-1
Reference
2  [PMID:4388687]
  Authors
Eady RR, Large PJ.
  Title
Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine.
  Journal
Biochem J 106:245-55 (1968)
Reference
3  [PMID:5124384]
  Authors
Eady RR, Large PJ.
  Title
Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM1.
  Journal
Biochem J 123:757-71 (1971)
Reference
4  [PMID:18512962]
  Authors
Cavalieri C, Biermann N, Vlasie MD, Einsle O, Merli A, Ferrari D, Rossi GL, Ubbink M
  Title
Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus.
  Journal
Biochemistry 47:6560-70 (2008)
DOI:10.1021/bi7023749
Reference
5  [PMID:20873742]
  Authors
Meschi F, Wiertz F, Klauss L, Cavalieri C, Blok A, Ludwig B, Heering HA, Merli A, Rossi GL, Ubbink M
  Title
Amicyanin transfers electrons from methylamine dehydrogenase to cytochrome c-551i via a ping-pong mechanism, not a ternary complex.
  Journal
J Am Chem Soc 132:14537-45 (2010)
DOI:10.1021/ja105498m
Other DBs
ExplorEnz - The Enzyme Database: 1.4.9.1
IUBMB Enzyme Nomenclature: 1.4.9.1
ExPASy - ENZYME nomenclature database: 1.4.9.1
UM-BBD (Biocatalysis/Biodegradation Database): 1.4.9.1
BRENDA, the Enzyme Database: 1.4.9.1

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