Amine dehydrogenase

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Amine Dehydrogenase (EC 1.4.99.3), also known as Methylamine Dehydrogenase, is a 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 prosthetic group.

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.

[edit] 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. 

[edit] External links

• MeSH methylamine+dehydrogenase

v • d • e CH-NH2 oxidoreductases (EC 1.4) - primarily amino acid oxidoreductases 1.4.1 - NAD/NADP acceptor Glutamate dehydrogenase (GLUD1) 1.4.3 - oxygen acceptor D-amino acid oxidase - Amine oxidase - Lysyl oxidase - Monoamine oxidase 1.4.4 - disulfide acceptor Glycine decarboxylase complex 1.4.99 - other acceptors D-amino acid dehydrogenase - Amine dehydrogenase