ENZYME entry: EC 1.17.9.1
| Accepted Name |
|---|
| 4-methylphenol dehydrogenase (hydroxylating).
|
| Alternative Name(s) |
|---|
| 4-cresol dehydrogenase (hydroxylating). |
| p-cresol methylhydroxylase. |
| p-cresol-(acceptor) oxidoreductase (hydroxylating). |
| Reaction catalysed |
|---|
| 4-methylphenol + 4 oxidized azurin + H(2)O <=> 4-hydroxybenzaldehyde + 4 reduced azurin + 4 H(+) |
| Comment(s) |
|---|
- 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 1.17.99.1.
|
| Cross-references |
|---|
| BRENDA | 1.17.9.1 |
| EC2PDB | 1.17.9.1 |
| ExplorEnz | 1.17.9.1 |
| PRIAM enzyme-specific profiles | 1.17.9.1 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.17.9.1 |
| IUBMB Enzyme Nomenclature | 1.17.9.1 |
| IntEnz | 1.17.9.1 |
| MEDLINE | Find literature relating to 1.17.9.1 |
| MetaCyc | 1.17.9.1 |
| UniProtKB/Swiss-Prot |
|
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