EC 1.4.9.1 - Methylamine dehydrogenase (amicyanin)

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IntEnz Enzyme Nomenclature
EC 1.4.9.1

Names

Accepted name:
methylamine dehydrogenase (amicyanin)
Other names:
amine:(acceptor) oxidoreductase (deaminating)
methylamine dehydrogenase
primary-amine dehydrogenase
MADH
primary-amine:(acceptor) oxidoreductase (deaminating)
amine dehydrogenase
Systematic name:
methylamine:amicyanin oxidoreductase (deaminating)

Reaction

Cofactor

Comments:

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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UM-BBD , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0052876
CAS Registry Number: 60496-14-2
UniProtKB/Swiss-Prot: (10) [show] [UniProt]

References

  1. De Beer, R., Duine, J.A., Frank, J., Jr. and Large, P.J.
    The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1: evidence for a quinone structure.
    Biochim. Biophys. Acta 622: 370-374 (1980). [PMID: 6246962]
  2. Eady, R.R. and Large, P.J.
    Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine.
    Biochem. J. 106: 245-255 (1968). [PMID: 4388687]
  3. Eady, R.R. and Large, P.J.
    Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM1.
    Biochem. J. 123: 757-771 (1971). [PMID: 5124384]
  4. Cavalieri, C., Biermann, N., Vlasie, M. D., Einsle, O., Merli, A., Ferrari, D., Rossi, G. L., Ubbink, M.
    Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus.
    Biochemistry 47: 6560-6570 (2008). [PMID: 18512962]
  5. Meschi, F., Wiertz, F., Klauss, L., Cavalieri, C., Blok, A., Ludwig, B., Heering, H. A., Merli, A., Rossi, G. L., Ubbink, M.
    Amicyanin transfers electrons from methylamine dehydrogenase to cytochrome c-551i via a ping-pong mechanism, not a ternary complex.
    J. Am. Chem. Soc. 132: 14537-14545 (2010). [PMID: 20873742]

[EC 1.4.98.1 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]