ENZYME entry: EC 18.104.22.168
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|4-methylphenol dehydrogenase (hydroxylating).
|4-cresol dehydrogenase (hydroxylating).|
|p-cresol-(acceptor) oxidoreductase (hydroxylating).|
|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 22.214.171.124.
|PRIAM enzyme-specific profiles||126.96.36.199|
|KEGG Ligand Database for Enzyme Nomenclature||188.8.131.52|
|IUBMB Enzyme Nomenclature||184.108.40.206|
|MEDLINE||Find literature relating to 220.127.116.11|
|Rhea expert-curated reactions||18.104.22.168|
entries corresponding to 1.17.9.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.17.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-