Methylamine dehydrogenase (amicyanin)

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

methylamine + H₂O + amicyanin

\rightleftharpoons

formaldehyde + ammonia + reduced amicyanin

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

References

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.
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.
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.
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.
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.

External links

Methylamine+dehydrogenase+(amicyanin) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e CH-NH₂ oxidoreductases (EC 1.4) - primarily amino acid oxidoreductases
1.4.1: NAD/NADP acceptor	Glutamate dehydrogenase GLUD1 GLUD2 Glutamate synthase (NADPH)
1.4.3: oxygen acceptor	D-amino acid oxidase Amine oxidase (Copper-containing (Lysyl Diamine Primary-amine)) (Flavin-containing (Monoamine)))
1.4.4: disulfide acceptor	Glycine cleavage system
1.4.99: other acceptors	D-amino acid dehydrogenase Amine dehydrogenase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 1.4.9