Camphor 5-monooxygenase

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
camphor 5-monooxygenase
Identifiers
EC number1.14.15.1
CAS number9030-82-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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

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.

Examples
Camphor 5-monooxygenase
Identifiers
OrganismPseudomonas putida
SymbolcamC
Alt. symbolscyp101
UniProtP00183
Other data
EC number1.14.15.1
Putidaredoxin
Identifiers
OrganismPseudomonas putida
SymbolcamB
Alt. symbolsPDX
UniProtP00259
Putidaredoxin reductase CamA
Identifiers
OrganismPseudomonas putida
SymbolcamA
Alt. symbolsPdr
UniProtP16640
Other data
EC number1.18.1.5

Cytochrome P450 camphor 5-monooxygenase is a bacterial enzyme originally from Pseudomonas putida, which catalyzes a critical step in the metabolism of camphor. In 1987, Cytochrome P450cam was the first cytochrome P450 three-dimensional protein structure solved by X-ray crystallography.[1]

It is a heterotrimeric protein derived from the products of three genes: a cytochrome P450 enzyme (encoded by the CamC gene from the CYP family CYP101), a Putidaredoxin (encoded by the CamB gene) complexed with cofactors 2Fe-2S, a NADH-dependent Putidaredoxin reductase (encoded by the CamA gene).[2]

References
  1. Poulos TL, Finzel BC, Howard AJ (June 1987). "High-resolution crystal structure of cytochrome P450cam". Journal of Molecular Biology. 195 (3): 687–700. doi:10.1016/0022-2836(87)90190-2. PMID 3656428.
  2. Li S, Wackett LP (September 1993). "Reductive dehalogenation by cytochrome P450CAM: substrate binding and catalysis". Biochemistry. 32 (36): 9355–61. doi:10.1021/bi00087a014. PMID 8369306.

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