Methylamine dehydrogenase (amicyanin)

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Methylamine dehydrogenase (amicyanin)
Identifiers
EC no. 1.4.9.1
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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 formaldehyde + ammonia + reduced amicyanin

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

References

  1. de Beer R, Duine JA, Frank J, Large PJ (April 1980). "The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1: evidence for a quinone structure". Biochimica et Biophysica Acta. 622 (2): 370–4. doi:10.1016/0005-2795(80)90050-1. PMID   6246962.
  2. Eady RR, Large PJ (January 1968). "Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine". The Biochemical Journal. 106 (1): 245–55. doi:10.1042/bj1060245. PMC   1198491 . PMID   4388687.
  3. Eady RR, Large PJ (August 1971). "Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM1". The Biochemical Journal. 123 (5): 757–71. doi:10.1042/bj1230757. PMC   1177077 . PMID   5124384.
  4. Cavalieri C, Biermann N, Vlasie MD, Einsle O, Merli A, Ferrari D, Rossi GL, Ubbink M (June 2008). "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. doi:10.1021/bi7023749. PMID   18512962.
  5. Meschi F, Wiertz F, Klauss L, Cavalieri C, Blok A, Ludwig B, Heering HA, Merli A, Rossi GL, Ubbink M (October 2010). "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. Bibcode:2010JAChS.13214537M. doi:10.1021/ja105498m. hdl: 11381/2328147 . PMID   20873742.