Aryl-alcohol dehydrogenase

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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⁺ $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1F8F.

[edit] References

IUBMB entry for 1.1.1.90
BRENDA references for 1.1.1.90 (Recommended.)
PubMed references for 1.1.1.90
PubMed Central references for 1.1.1.90
Google Scholar references for 1.1.1.90
Suhara K, Takemori S, Katagiri M (1969). "The purification and properties of benzylalcohol dehydrogenase from Pseudomonas sp". Arch. Biochem. Biophys. 130: 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: 1161–1171.