Aryl-alcohol dehydrogenase
| aryl-alcohol dehydrogenase | |||||||||
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| Identifiers | |||||||||
| EC number | 1.1.1.90 | ||||||||
| CAS number | 37250-26-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, an aryl-alcohol dehydrogenase (EC 1.1.1.90) is an enzyme that catalyzes the chemical reaction
- an aromatic alcohol + NAD+
an aromatic aldehyde + NADH + H+
Thus, the two substrates of this enzyme are aromatic alcohol and NAD+, whereas its 3 products are aromatic aldehyde, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is aryl-alcohol:NAD+ oxidoreductase. Other names in common use include p-hydroxybenzyl alcohol dehydrogenase, benzyl alcohol dehydrogenase, and coniferyl alcohol dehydrogenase. This enzyme participates in 5 metabolic pathways: tyrosine metabolism, phenylalanine metabolism, biphenyl degradation, toluene and xylene degradation, and caprolactam degradation.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1F8F.
References
- Suhara K, Takemori S, Katagiri M (1969). "The purification and properties of benzylalcohol dehydrogenase from Pseudomonas sp". Arch. Biochem. Biophys. 130 (1): 422–9. doi:10.1016/0003-9861(69)90054-X. PMID 5778658.
- Yamanaka K and Minoshima R (1984). "Identification and characterization of a nicotinamide adenine dinucleotide-dependent para-hydroxybenzyl alcohol-dehydrogenase from Rhodopseudomonas acidophila M402". Agric. Biol. Chem. 48 (5): 1161–1171. doi:10.1271/bbb1961.48.1161.
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