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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.
References
- Davidson VL (2004). "Electron transfer in quinoproteins". Arch. Biochem. Biophys. 428 (1): 32–40. doi:. PMID 15234267.
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