Camphor 5-monooxygenase

camphor 5-monooxygenase
Catalytic complex between Pseudomonas putida camphor 5-monooxygenase (red) and putidaredoxin (blue) PDB: 5GXG ​
Identifiers
EC no.	1.14.15.1
CAS no.	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
Search PMC articles PubMed articles NCBI proteins

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

(+)-camphor + putidaredoxin + O₂${\displaystyle \rightleftharpoons }$ (+)-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 of 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
Organism	Pseudomonas putida
Symbol	camC
Alt. symbols	cyp101
UniProt	P00183
Other data
EC number	1.14.15.1
Search for Structures Swiss-model Domains InterPro

Putidaredoxin
Identifiers
Organism	Pseudomonas putida
Symbol	camB
Alt. symbols	PDX
UniProt	P00259
Search for Structures Swiss-model Domains InterPro

Putidaredoxin reductase CamA
Identifiers
Organism	Pseudomonas putida
Symbol	camA
Alt. symbols	Pdr
UniProt	P16640
Other data
EC number	1.18.1.5
Search for Structures Swiss-model Domains InterPro

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.