Amine dehydrogenase
| Amine dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
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
[edit]- 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
[edit]- methylamine+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
 | This enzyme-related article is a stub. You can help Wikipedia by expanding it. |