Aralkylamine dehydrogenase (azurin)
| Aralkylamine dehydrogenase (azurin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.4.9.2 | ||||||||
| 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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Aralkylamine dehydrogenase (azurin) (EC 1.4.9.2, aromatic amine dehydrogenase, arylamine dehydrogenase, tyramine dehydrogenase) is an enzyme with the systematic name aralkylamine:azurin oxidoreductase (deaminating).[1][2][3][4][5] This enzyme catalyses the following chemical reaction:
- ArCH2NH2 + H2O + 2 azurin ArCHO + NH3 + 2 reduced azurin
The three substrates of this enzyme are RCH2NH2 (i.e., an aromatic amine), water, and the acceptor azurin, and its three products are RCHO, ammonia, and a reduced acceptor. Azurin can be replaced with the artificial acceptor phenazine methosulfate in in vitro studies.[1]
This quinoprotein enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with other acceptors. This enzyme participates in tyrosine metabolism and phenylalanine metabolism. It is notable for its chemical mechanism, which is dominated by proton tunneling.[6]
References
- 1 2 Iwaki, M.; Yagi, T.; Horiike, K.; Saeki, Y.; Ushijima, T.; Nozaki, M. (1983). "Crystallization and properties of aromatic amine dehydrogenase from Pseudomonas sp". Arch. Biochem. Biophys. 220: 253–262. PMID 6830237. doi:10.1016/0003-9861(83)90408-3.
- ↑ Hyun, Y.L.; Davidson, V.L. (1995). "Electron transfer reactions between aromatic amine dehydrogenase and azurin". Biochemistry. 34 (38): 12249–12254. PMID 7547967. doi:10.1021/bi00038a020.
- ↑ Hyun, Y.L.; Zhu, Z.; Davidson, V.L. (1999). "Gated and ungated electron transfer reactions from aromatic amine dehydrogenase to azurin". J. Biol. Chem. 274 (41): 29081–29086. PMID 10506161. doi:10.1074/jbc.274.41.29081.
- ↑ Davidson, V.L. (2004). "Electron transfer in quinoproteins". Arch. Biochem. Biophys. 428 (1): 32–40. PMID 15234267. doi:10.1016/j.abb.2004.03.022.
- ↑ Sukumar, N.; Chen, Z.W.; Ferrari, D.; Merli, A.; Rossi, G.L.; Bellamy, H.D.; Chistoserdov, A.; Davidson, V.L.; Mathews, F.S. (2006). "Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis". Biochemistry. 45 (45): 13500–13510. PMID 17087503. doi:10.1021/bi0612972.
- ↑ Masgrau, L; Roujeinikova, A; Johannissen, LO; Hothi, P; Basran, J; Ranaghan, KE; Mulholland, AJ; Sutcliffe, MJ; Scrutton, NS; Leys, D (14 April 2006). "Atomic description of an enzyme reaction dominated by proton tunneling.". Science. 312 (5771): 237–41. PMID 16614214. doi:10.1126/science.1126002.