4-hydroxybenzaldehyde dehydrogenase

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4-hydroxybenzaldehyde dehydrogenase
Identifiers
EC no. 1.2.1.64
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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PMC articles
PubMed articles
NCBI proteins

In enzymology, 4-hydroxybenzaldehyde dehydrogenase (EC 1.2.1.64) is an enzyme that catalyzes the chemical reaction

+ NAD+
 
 
H2O
H+
4-hydroxybenzaldehyde dehydrogenase
H2O
H+
 
+ NADH
 

The three substrates of this enzyme are 4-hydroxybenzaldehyde, oxidised nicotinamide adenine dinucleotide (NAD+), and water. Its products are 4-hydroxybenzoic acid, reduced NADH, and a proton. [1]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-hydroxybenzaldehyde:NAD+ oxidoreductase. This enzyme is also called p-hydroxybenzaldehyde dehydrogenase. This enzyme participates in toluene and xylene degradation in bacteria. [2] [3] It is also found in carrots ( Daucus carota ). [4]

References

  1. Enzyme 1.2.1.64 at KEGG Pathway Database.
  2. Bossert ID, Whited G, Gibson DT, Young LY (1989). "Anaerobic oxidation of p-cresol mediated by a partially purified methylhydroxylase from a denitrifying bacterium". J. Bacteriol. 171 (6): 2956–62. doi:10.1128/jb.171.6.2956-2962.1989. PMC   210000 . PMID   2722739.
  3. Whited GM, Gibson DT (1991). "Separation and partial characterization of the enzymes of the toluene-4-monooxygenase catabolic pathway in Pseudomonas mendocina KR1". J. Bacteriol. 173 (9): 3017–20. doi:10.1128/jb.173.9.3017-3020.1991. PMC   207886 . PMID   2019564.
  4. Sircar, D.; Mitra, A. (2008). "Evidence for p-hydroxybenzoate formation involving enzymatic phenylpropanoid side-chain cleavage in hairy roots of Daucus carota". Journal of Plant Physiology. 165 (4): 407–414. Bibcode:2008JPPhy.165..407S. doi:10.1016/j.jplph.2007.05.005. PMID   17658659.