Aryl-alcohol dehydrogenase
| aryl-alcohol dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.90 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
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
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1F8F.
References
[edit]- 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; 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.
