Camphor 5-monooxygenase

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camphor 5-monooxygenase
Identifiers
EC number 1.14.15.1
CAS number 9030-82-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

In enzymology, a camphor 5-monooxygenase (EC 1.14.15.1) is an enzyme that catalyzes the chemical reaction

(+)-camphor + putidaredoxin + O2 (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O

The 3 substrates of this enzyme are (+)-camphor, putidaredoxin, and O2, whereas its 3 products are (+)-exo-5-hydroxycamphor, oxidized putidaredoxin, and H2O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen, the oxygen incorporated need not be derived from O2 with reduced iron-sulfur protein as one donor, and incorporation o one atom of oxygen into the other donor. The systematic name of this enzyme class is (+)-camphor,reduced putidaredoxin:oxygen oxidoreductase (5-hydroxylating). Other names in common use include camphor 5-exo-methylene hydroxylase, 2-bornanone 5-exo-hydroxylase, bornanone 5-exo-hydroxylase, camphor 5-exo-hydroxylase, camphor 5-exohydroxylase, camphor hydroxylase, d-camphor monooxygenase, methylene hydroxylase, methylene monooxygenase, D-camphor-exo-hydroxylase, and camphor methylene hydroxylase. It employs one cofactor, heme.

Structural studies[edit]

As of late 2007, 58 structures have been solved for this class of enzymes, with PDB accession codes 1AKD, 1C8J, 1CP4, 1GEB, 1GEK, 1GEM, 1GJM, 1IWI, 1IWJ, 1IWK, 1J51, 1K2O, 1LWL, 1MPW, 1NOO, 1O76, 1P2Y, 1P7R, 1PHA, 1PHB, 1PHC, 1PHD, 1PHE, 1PHF, 1PHG, 1QMQ, 1RE9, 1RF9, 1T85, 1T86, 1T87, 1T88, 1YRC, 1YRD, 2A1M, 2A1N, 2A1O, 2CP4, 2CPP, 2FE6, 2FER, 2FEU, 2FRZ, 2GQX, 2GR6, 2H7Q, 2H7R, 2H7S, 3CP4, 3CPP, 4CP4, 4CPP, 5CP4, 5CPP, 6CP4, 6CPP, 7CPP, and 8CPP.

References[edit]

  • Hedegaard J, Gunsalus IC (1965). "Mixed function oxidation. IV. An induced methylene hydroxylase in camphor oxidation". J. Biol. Chem. 240 (10): 4038–43. PMID 4378858. 
  • Tyson CA, Lipscomb JD, Gunsalus IC (1972). "The role of putidaredoxin and P450 cam in methylene hydroxylation". J. Biol. Chem. 247 (18): 5777–84. PMID 4341491.