Amine dehydrogenase
Amine dehydrogenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.4.99.3 | ||||||||
CAS no. | 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 | ||||||||
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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 (August 2004). "Electron transfer in quinoproteins". Archives of Biochemistry and Biophysics. 428 (1): 32–40. doi:10.1016/j.abb.2004.03.022. PMID 15234267.
External links
- methylamine+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- v
- t
- e
- Glutamate dehydrogenase
- Glutamate synthase (NADPH)
- D-amino acid oxidase
- Amine oxidase (Copper-containing (Lysyl
- Diamine
- Primary-amine)) (Flavin-containing (Monoamine)))
- D-amino acid dehydrogenase
- Amine dehydrogenase
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