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).^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

methylamine + H₂O + amicyanin

\rightleftharpoons

formaldehyde + ammonia + reduced amicyanin

This enzyme contains tryptophan tryptophylquinone (TTQ) cofactor.

References

↑ De Beer, R., Duine, J.A., Frank, J., Jr. and Large, P.J. (1980). "The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1: evidence for a quinone structure". Biochim. Biophys. Acta 622 (2): 370–374. doi:10.1016/0005-2795(80)90050-1. PMID 6246962.
↑ Eady, R.R. and Large, P.J. (1968). "Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine". Biochem. J. 106 (1): 245–255. PMC 1198491. PMID 4388687.
↑ Eady, R.R. and Large, P.J. (1971). "Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM1". Biochem. J. 123 (5): 757–771. PMC 1177077. PMID 5124384.
↑ Cavalieri, C., Biermann, N., Vlasie, M.D., Einsle, O., Merli, A., Ferrari, D., Rossi, G.L. and Ubbink, M. (2008). "Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus". Biochemistry 47 (25): 6560–6570. doi:10.1021/bi7023749. PMID 18512962.
↑ Meschi, F., Wiertz, F., Klauss, L., Cavalieri, C., Blok, A., Ludwig, B., Heering, H.A., Merli, A., Rossi, G.L. and Ubbink, M. (2010). "Amicyanin transfers electrons from methylamine dehydrogenase to cytochrome c-551i via a ping-pong mechanism, not a ternary complex". J. Am. Chem. Soc. 132 (41): 14537–14545. doi:10.1021/ja105498m. PMID 20873742.

External links

Methylamine dehydrogenase (amicyanin) at the US National Library of Medicine Medical Subject Headings (MeSH)

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

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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