Biology:Methylamine dehydrogenase (amicyanin)

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Methylamine dehydrogenase (amicyanin)
Identifiers
EC number1.4.9.1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Methylamine dehydrogenase (amicyanin) (EC 1.4.9.1, amine dehydrogenase, primary-amine dehydrogenase) is an enzyme with systematic name methylamine:amicyanin oxidoreductase (deaminating).[1][2][3][4][5] This enzyme catalyses the following chemical reaction:

methylamine + H2O + amicyanin [math]\displaystyle{ \rightleftharpoons }[/math] formaldehyde + ammonia + reduced amicyanin

This enzyme contains tryptophan tryptophylquinone (TTQ) co-factor.

References

  1. "The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1: evidence for a quinone structure". Biochimica et Biophysica Acta 622 (2): 370–4. April 1980. doi:10.1016/0005-2795(80)90050-1. PMID 6246962. 
  2. "Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine". The Biochemical Journal 106 (1): 245–55. January 1968. doi:10.1042/bj1060245. PMID 4388687. 
  3. "Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM1". The Biochemical Journal 123 (5): 757–71. August 1971. doi:10.1042/bj1230757. PMID 5124384. 
  4. "Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus". Biochemistry 47 (25): 6560–70. June 2008. doi:10.1021/bi7023749. PMID 18512962. https://figshare.com/articles/journal_contribution/2857966. 
  5. "Amicyanin transfers electrons from methylamine dehydrogenase to cytochrome c-551i via a ping-pong mechanism, not a ternary complex". Journal of the American Chemical Society 132 (41): 14537–45. October 2010. doi:10.1021/ja105498m. PMID 20873742. 

External links