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ENZYME

ENZYME entry: EC 1.14.15.25

PURL: https://purl.expasy.org/enzyme/EC/1.14.15.25
Accepted Name
p-cymene methyl-monooxygenase
Alternative Name(s)
p-cymene methyl hydroxylase
Reaction catalysed
p-cymene + 2 reduced [2Fe-2S]-[ferredoxin] + O2 + 2 H(+) = 4-isopropylbenzyl alcohol + 2 oxidized [2Fe-2S]-[ferredoxin] + H2O
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
KEGG Ligand Database for Enzyme Nomenclature1.14.15.25
IUBMB Enzyme Nomenclature1.14.15.25
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.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-