Amine dehydrogenase

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Amine Dehydrogenase (EC 1.4.99.3), also known as methylamine dehydrogenase (MADH), is a tryptophan tryptophylquinone-dependent (TTQ-dependent) enzyme that catalyzes the oxidative deamination of a primary amine to an aldehyde and ammonia. The reaction occurs as follows:

RCH₂NH₂ + H₂O + acceptor → RCHO + NH₃ + reduced acceptor

Amine dehydrogenase possesses an α₂β₂ structure with each smaller β subunit possessing a TTQ protein cofactor.

Amine dehydrogenase, studied in Paracoccus denitrificans, at least transiently forms a ternary complex to catalyze methylamine-dependent cytochrome c-551i reduction. Within this complex, electrons are transferred from the TTQ cofactor of MADH to the Type 1 copper center of amicyanin, and then to the heme of the cytochrome.

References

Davidson VL (2004). "Electron transfer in quinoproteins". Arch. Biochem. Biophys. 428 (1): 32–40. doi:10.1016/j.abb.2004.03.022. PMID 15234267.

External links

methylamine dehydrogenase 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

Proteins: 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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