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ENZYME entry: EC 1.14.15.25

Accepted Name
p-cymene methyl-monooxygenase.
Alternative Name(s)
p-cymene methyl hydroxylase.
Reaction catalysed
p-cymene + O(2) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) <=> 4-isopropylbenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O
Comment(s)
  • The enzyme, characterized from several Pseudomonas strains, initiates p-cymene catabolism through hydroxylation of the methyl group.
  • The enzyme has a distinct preference for substrates containing at least an alkyl or heteroatom substituent at the para-position of toluene.
  • The electrons are provided by a reductase (EC 1.18.1.3) that transfers electrons from NADH via FAD and an [2Fe-2S] cluster.
  • In Pseudomonas chlororaphis the presence of a third component of unknown function greatly increases the activity.
  • Cf. EC 1.14.15.26.
Cross-references
BRENDA1.14.15.25
EC2PDB1.14.15.25
ExplorEnz1.14.15.25
PRIAM enzyme-specific profiles1.14.15.25
KEGG Ligand Database for Enzyme Nomenclature1.14.15.25
IUBMB Enzyme Nomenclature1.14.15.25
IntEnz1.14.15.25
MEDLINEFind literature relating to 1.14.15.25
MetaCyc1.14.15.25
Rhea expert-curated reactions1.14.15.25

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.15.-
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