Aralkylamine dehydrogenase (azurin)
| Aralkylamine dehydrogenase (azurin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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
[edit]- ^ a b Iwaki M, Yagi T, Horiike K, Saeki Y, Ushijima T, Nozaki M (January 1983). "Crystallization and properties of aromatic amine dehydrogenase from Pseudomonas sp". Archives of Biochemistry and Biophysics. 220 (1): 253–62. doi:10.1016/0003-9861(83)90408-3. PMID 6830237.
- ^ Hyun YL, Davidson VL (September 1995). "Electron transfer reactions between aromatic amine dehydrogenase and azurin". Biochemistry. 34 (38): 12249–54. doi:10.1021/bi00038a020. PMID 7547967.
- ^ Hyun YL, Zhu Z, Davidson VL (October 1999). "Gated and ungated electron transfer reactions from aromatic amine dehydrogenase to azurin". The Journal of Biological Chemistry. 274 (41): 29081–6. doi:10.1074/jbc.274.41.29081. PMID 10506161.
- ^ 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.
- ^ Sukumar N, Chen ZW, Ferrari D, Merli A, Rossi GL, Bellamy HD, Chistoserdov A, Davidson VL, Mathews FS (November 2006). "Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis". Biochemistry. 45 (45): 13500–10. doi:10.1021/bi0612972. PMID 17087503.
- ^ Masgrau L, Roujeinikova A, Johannissen LO, Hothi P, Basran J, Ranaghan KE, Mulholland AJ, Sutcliffe MJ, Scrutton NS, Leys D (April 2006). "Atomic description of an enzyme reaction dominated by proton tunneling". Science. 312 (5771): 237–41. Bibcode:2006Sci...312..237M. doi:10.1126/science.1126002. PMID 16614214. S2CID 27201250.
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