• Source: 4-Cresol dehydrogenase (hydroxylating)

In enzymology, a 4-cresol dehydrogenase (hydroxylating) (EC 1.17.99.1) is an enzyme that catalyzes the chemical reaction

4-cresol + acceptor + H2O



⇌


{\displaystyle \rightleftharpoons }

4-hydroxybenzaldehyde + reduced acceptor
The 3 substrates of this enzyme are 4-cresol, acceptor, and H2O, whereas its two products are 4-hydroxybenzaldehyde and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with other acceptors. The systematic name of this enzyme class is 4-cresol:acceptor oxidoreductase (methyl-hydroxylating). Other names in common use include p-cresol–(acceptor) oxidoreductase (hydroxylating), and p-cresol methylhydroxylase. This enzyme participates in toluene and xylene degradation. It has 2 cofactors: FAD, and Cytochrome c.




Structural studies


As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1DII, 1DIQ, 1WVE, and 1WVF.




References



Hopper DJ, Taylor DG (1977). "The Purification and Properties of p-cresol–(Acceptor) Oxidoreductase (Hydroxylating), a Flavocytochrome from Pseudomonas putida". Biochem. J. 167 (1): 155–62. doi:10.1042/bj1670155. PMC 1183632. PMID 588247.
McIntire W, Edmondson DE, Singer TP, Hopper DJ (1980). "8α-O-Tyrosyl-FAD: A New Form of Covalently Bound Flavin from p-Cresol Methylhydroxylase". J. Biol. Chem. 255 (14): 6553–5. doi:10.1016/S0021-9258(18)43602-2. PMID 7391034.

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• 4-Cresol dehydrogenase (hydroxylating)
• Index of molecular biology articles
• Hydrocarbonoclastic bacteria