Biology: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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
- ↑ 1.0 1.1 "Crystallization and properties of aromatic amine dehydrogenase from Pseudomonas sp". Archives of Biochemistry and Biophysics 220 (1): 253–62. January 1983. doi:10.1016/0003-9861(83)90408-3. PMID 6830237.
- ↑ "Electron transfer reactions between aromatic amine dehydrogenase and azurin". Biochemistry 34 (38): 12249–54. September 1995. doi:10.1021/bi00038a020. PMID 7547967.
- ↑ "Gated and ungated electron transfer reactions from aromatic amine dehydrogenase to azurin". The Journal of Biological Chemistry 274 (41): 29081–6. October 1999. doi:10.1074/jbc.274.41.29081. PMID 10506161.
- ↑ "Electron transfer in quinoproteins". Archives of Biochemistry and Biophysics 428 (1): 32–40. August 2004. doi:10.1016/j.abb.2004.03.022. PMID 15234267.
- ↑ "Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis". Biochemistry 45 (45): 13500–10. November 2006. doi:10.1021/bi0612972. PMID 17087503.
- ↑ "Atomic description of an enzyme reaction dominated by proton tunneling". Science 312 (5771): 237–41. April 2006. doi:10.1126/science.1126002. PMID 16614214. Bibcode: 2006Sci...312..237M.
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