CATH Classification
Domain Context
CATH Clusters
| Superfamily | Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2 |
| Functional Family |
Enzyme Information
| 1.17.9.1 |
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 1.17.99.1.
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UniProtKB Entries (1)
| P09787 |
CY4C_PSEPU
Pseudomonas putida
4-cresol dehydrogenase [hydroxylating] cytochrome c subunit
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PDB Structure
| PDB | 1DIQ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| 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.
J.Mol.Biol.
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