Methylamine_dehydrogenase_(amicyanin)

Methylamine dehydrogenase (amicyanin)

Methylamine dehydrogenase (amicyanin)

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

References

  1. [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. [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. [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. [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. [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. doi:10.1021/ja105498m. hdl:11381/2328147. PMID 20873742.
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