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 + amicyanin = formaldehyde + ammonia + reduced amicyanin [RN:R00606]
Reaction(KEGG)
Substrate
methylamine [CPD:C00218];
H2O [CPD:C00001];
amicyanin [CPD:C19671]
Product
formaldehyde [CPD:C00067];
ammonia [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.
Pathway
Methane metabolism
Microbial metabolism in diverse environments
Orthology
K08685  
quinohemoprotein amine dehydrogenase
K15228  
methylamine dehydrogenase light chain
K15229  
methylamine dehydrogenase heavy chain
Genes
VFU: 
PPF: 
PPG: 
PPW: 
PFL: 
PFL_4120(peaA)
PFO: 
PEN: 
PMK: 
PAT: 
GAG: 
ADI: 
B5T_00161 B5T_00164 B5T_00533 B5T_00536
PSE: 
NH8B_2195
REU: 
Reut_B4077 Reut_B4080
BUR: 
Bcep18194_B0601 Bcep18194_B0604
BCN: 
Bcen_3305 Bcen_3308
BCH: 
Bcen2424_5059 Bcen2424_5062
BCM: 
Bcenmc03_5222 Bcenmc03_5225
BCJ: 
BCAM2301 BCAM2304
BAM: 
Bamb_4469 Bamb_4472
BAC: 
BamMC406_4994 BamMC406_4997
BMU: 
Bmul_3580 Bmul_3583
BMJ: 
BMULJ_04934 BMULJ_04937
BCT: 
GEM_3380 GEM_3383
BPH: 
Bphy_3809 Bphy_3812
BGE: 
BC1002_1587 BC1002_1590
BGF: 
BC1003_3869 BC1003_3872
BYI: 
BYI23_B006010 BYI23_B006040
AXY: 
AXYL_02123 AXYL_02126
AKA: 
TKWG_18915 TKWG_18935
MPT: 
Mpe_A2653
EBA: 
ebA2235(qhpA)
AZO: 
azo1239(qhpA) azo2257(mauA) azo2260(maub)
TMZ: 
Tmz1t_0761
MFA: 
Mfla_0548 Mfla_0551
MMB: 
Mmol_1572 Mmol_1575
ABU: 
Abu_0465
MEA: 
Mex_1p2770(mauB) Mex_1p2773(mauA)
MCH: 
Mchl_0562 Mchl_0565
PHL: 
KKY_2939 KKY_2942
CAK: 
Caul_0557 Caul_0560
PDE: 
Pden_1703 Pden_4730 Pden_4733
HBA: 
Hbal_2737 Hbal_2741
NAR: 
Saro_1685 Saro_1688 Saro_3028 Saro_3818 Saro_3821
NPP: 
PP1Y_Mpl7173 PP1Y_Mpl7192
SWI: 
Swit_3251 Swit_3254 Swit_4363 Swit_4365
SPHM: 
G432_07310 G432_07325
GDI: 
GDI_0271(mauB) GDI_0273(mauA) GDI_1806(mauB) GDI_1807(mauA)
GDJ: 
Gdia_0036 Gdia_2335 Gdia_2337
APT: 
APA01_04540 APA01_04570
APW: 
APA42C_04540 APA42C_04570
APF: 
APA03_04540 APA03_04570
APU: 
APA07_04540 APA07_04570
APG: 
APA12_04540 APA12_04570
APQ: 
APA22_04540 APA22_04570
APX: 
APA26_04540 APA26_04570
APZ: 
APA32_04540 APA32_04570
PGV: 
SL003B_2489
RER: 
RER_53630
REQ: 
REQ_44990(mauA)
MIN: 
Minf_1997 Minf_2000
 » 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 (1980) 370-4.
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 (1968) 245-55.
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 (1971) 757-71.
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 (2008) 6560-70.
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 (2010) 14537-45.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
DBGET integrated database retrieval system