Amine Dehydrogenase (EC 22.214.171.124), 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:
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.
- Davidson VL (2004). "Electron transfer in quinoproteins". Arch. Biochem. Biophys. 428 (1): 32–40. doi:10.1016/j.abb.2004.03.022. PMID 15234267.
CH-NH2 oxidoreductases (EC 1.4) - primarily amino acid oxidoreductases 1.4.1: NAD/NADP acceptor 1.4.3: oxygen acceptor 1.4.4: disulfide acceptor 1.4.99: other acceptorsD-amino acid dehydrogenase - Amine dehydrogenase This article about an organic compound is a stub. You can help Wikipedia by expanding it. This enzyme-related article is a stub. You can help Wikipedia by expanding it.