CATH Classification

Domain Context

CATH Clusters

Superfamily FAD-linked oxidases, C-terminal domain
Functional Family

Enzyme Information
4-methylphenol dehydrogenase (hydroxylating).
based on mapping to UniProt P09788
4-methylphenol + 4 oxidized azurin + H(2)O = 4-hydroxybenzaldehyde + 4 reduced azurin + 4 H(+).
-!- This bacterial enzyme contains a flavin (FAD) subunit and a cytochrome c subunit. -!- The flavin subunit abstracts two hydrogen atoms from the substrate, forming a quinone methide intermediate, then hydrates the latter at the benzylic carbon with a hydroxyl group derived from water. -!- The protons are lost to the bulk solvent, while the electrons are passed to the heme on the cytochrome subunit, and from there to azurin, a small copper-binding protein that is co-localized with the enzyme in the periplasm. -!- The first hydroxylation forms 4-hydroxybenzyl alcohol; a second hydroxylation converts this into 4-hydroxybenzaldehyde. -!- Formerly EC

UniProtKB Entries (1)

Pseudomonas putida
4-cresol dehydrogenase [hydroxylating] cytochrome c subunit

PDB Structure

External Links
Primary Citation
Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism.
Cunane, L.M., Chen, Z.W., Shamala, N., Mathews, F.S., Cronin, C.N., McIntire, W.S.