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.
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
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: 
PRE: 
PKC: 
PKB_2656(mauA) PKB_2659(mauB)
PAT: 
GAG: 
ADI: 
PSE: 
REU: 
BUR: 
BCN: 
BCH: 
BCM: 
BCJ: 
BAM: 
BAC: 
BMU: 
BMJ: 
BCT: 
BPH: 
BGE: 
BGF: 
BYI: 
BUO: 
AXY: 
AXO: 
AXN: 
AKA: 
AMIM: 
CDN: 
MPT: 
EBA: 
ebA2235(qhpA)
AZO: 
azo1239(qhpA) azo2257(mauA) azo2260(maub)
TMZ: 
MFA: 
MMB: 
ABU: 
MEA: 
MCH: 
HNI: 
PHL: 
CAK: 
PDE: 
PAMI: 
HBA: 
NAR: 
NPP: 
SWI: 
SPHM: 
GDI: 
GDI_0271(mauB) GDI_0273(mauA) GDI_1806(mauB) GDI_1807(mauA)
GDJ: 
GXL: 
APT: 
APW: 
APF: 
APU: 
APG: 
APQ: 
APX: 
APZ: 
APK: 
PGV: 
RER: 
REY: 
REQ: 
REQ_44990(mauA)
RPY: 
MIN: 
 » 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: 

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