Amine dehydrogenase

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Amine dehydrogenase
Identifiers
EC number 1.4.99.3
CAS number 60496-14-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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.

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