3-hydroxybenzyl-alcohol dehydrogenase
In enzymology, a 3-hydroxybenzyl-alcohol dehydrogenase (EC 1.1.1.97) is an enzyme that catalyzes the chemical reaction
- 3-hydroxybenzyl alcohol + NADP+ 3-hydroxybenzaldehyde + NADPH + H+
3-hydroxybenzyl-alcohol dehydrogenase | |||||||||
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Identifiers | |||||||||
EC number | 1.1.1.97 | ||||||||
CAS number | 9075-73-4 | ||||||||
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 | ||||||||
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Thus, the two substrates of this enzyme are 3-hydroxybenzyl alcohol and NADP+, whereas its 3 products are 3-hydroxybenzaldehyde, NADPH, 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 3-hydroxybenzyl-alcohol:NADP+ oxidoreductase. Other names in common use include m-hydroxybenzyl alcohol dehydrogenase, m-hydroxybenzyl alcohol (NADP+) dehydrogenase, and m-hydroxybenzylalcohol dehydrogenase. This enzyme participates in toluene and xylene degradation.
References
- Forrester PI, Gaucher GM (1972). "m-Hydroxybenzyl alcohol dehydrogenase from Penicillium urticae". Biochemistry. 11 (6): 1108–14. doi:10.1021/bi00756a026. PMID 4335290.
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