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Chemical Compound Review

D-CAMPHOR     (1R,4R)-1,7,7- trimethylbicyclo[2.2.1]hepta. ..

Synonyms: Camphor(D), Camphor (1R), CPD-862, SureCN16069, CHEMBL504760, ...
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Disease relevance of camphor

  • Chronic camphor ingestion mimicking Reye's syndrome [1].
  • Camphor hydroxylase of Pseudomonas putida: vestiges of sequence homology in cytochrome P-450CAM, putidaredoxin, and related proteins [2].
  • E. coli cells expressing the triple fusion protein thus constitute the first heterologous self-sufficient catalytic system for the oxidation of camphor and other substrates by P450cam [3].
  • The enzyme 6-oxocamphor hydrolase, which catalyzes the desymmetrization of 6-oxocamphor to yield (2R,4S)-alpha-campholinic acid, has been purified with a factor of 35.7 from a wild type strain of Rhodococcus sp. NCIMB 9784 grown on (1R)-(+)-camphor as the sole carbon source [4].
  • Lack of regio- and stereospecificity in oxidation of (+) camphor by Streptomyces griseus enriched in cytochrome P-450soy [5].

Psychiatry related information on camphor

  • In the presence of artificial UV-light the highly photosensitive camphor was almost totally degraded after reaction times of 60 min [6].
  • 2) Patients who have ingested more than 30 mg/kg of a camphor-containing product or who are exhibiting symptoms of moderate to severe toxicity (e.g., convulsions, lethargy, ataxia, severe nausea and vomiting) by any route of exposure should be referred to an emergency department for observation and treatment (Grade D) [7].

High impact information on camphor

  • Structures were obtained for three intermediates in the hydroxylation reaction of camphor by P450cam with trapping techniques and cryocrystallography [8].
  • The mutants were selected as resistant to camphor vapors, which results in increased ploidy, and were subsequently screened for an increase in cell density and an increase in the gene dosage of the lac operon [9].
  • I have applied Kirkwood-Buff theory to calculate water numbers for two processes: (i) the allosteric transition of hemoglobin and (ii) the binding of camphor to cytochrome P450 [10].
  • The amino acid sequences of cytochrome P-450CAM and putidaredoxin of the camphor hydroxylase [camphor, reduced-putida-ferredoxin:oxygen oxidoreductase (5-hydroxylating), EC] of Pseudomonas putida are compared to each other and then to the sequences of bovine adrenodoxin and cytochrome b5 [2].
  • Synthesis and application in asymmetric catalysis of camphor-based pyridine ligands [11].

Chemical compound and disease context of camphor

  • Cytochrome P-450cam catalyzes the stereospecific methylene hydroxylation of camphor to form 5-exohydroxycamphor and is encoded by the camC gene on the CAM plasmid of Pseudomonas putida, ATCC 17453 [12].
  • At an extrapolated zero concentration of dye, the bacterial cytochrome from Pseudomonas putida catalyzing the hydroxylation of camphor and the adrenal mitochondrial cytochrome catalyzing the cholesterol side-chain cleavage reaction had formal reduction potentials of -168 and -285 mV (pH 7.5 and 25 degrees C), respectively [13].
  • P-450 from Pseudomonas linalool shows a much weaker dependence on pressure than P-450 from P. putida which has camphor as substrate [14].
  • Intact cells of (+/-)camphor-grown Pseudomonas putida, ATCC17453(CAM), have been shown to oxidize readily the monoketone derivative of cage hydrocarbon adamantane, forming oxygenated products indicative of both biological Baeyer-Villiger and hydroxylation reactions [15].
  • Other components of A. annua, camphor and 1,8-cineole, at 119 ppm also protected weight gains, and reduced E. tenella lesion scores [16].

Biological context of camphor

  • Models of the substrate, 6-oxo camphor, and a proposed enolate intermediate in the putative active site suggest possible mechanistic roles for Glu-244, Asp-154, His-122, His-45, and His-145 [17].
  • The drastic difference in the geminate kinetics suggests that the presence of camphor significantly alters the CO rebinding and escape rates by modifying the heme pocket environment [18].
  • The gene is closely associated with an open reading frame encoding a ferredoxin reductase that may be involved in the initial step in the biodegradation of camphor [4].
  • We have studied the interaction of a substrate analog of camphor, 5-exo-bromocamphor, with this cytochrome P-450 mixed function oxidase system in order to probe the molecular mechanisms of electron transport and catalytic substrate oxygenation [19].
  • Probing the interactions of putidaredoxin with redox partners in camphor P450 5-monooxygenase by mutagenesis of surface residues [20].

Anatomical context of camphor


Associations of camphor with other chemical compounds


Gene context of camphor

  • These activities were augmented when crcB was overexpressed with cspE (100-fold camphor resistance and 2.1-fold induction of rcsA) [30].
  • The authors have previously shown that overexpression of the Escherichia coli K-12 crcA, cspE and crcB genes protects the chromosome from decondensation by camphor [30].
  • A number of analogues in the TP series that incorporate a modified or unmodified L-methionine sulfone amide at the C2 endo position on the camphor ring exhibit high affinity for OT receptors (IC50 = 1.3-15 nM) and good selectivity for binding to OT versus arginine vasopressin V1a and V2 receptors [31].
  • Similar camphor-activated TRPV1-like currents were observed in isolated rat DRG neurons and were strongly potentiated after activation of protein kinase C with phorbol-12-myristate-13-acetate [32].
  • Conversely, TRPV3 current sensitized after repeated camphor applications, which is inconsistent with the analgesic role of camphor [32].

Analytical, diagnostic and therapeutic context of camphor

  • Camphor intoxication treated by resin hemoperfusion [33].
  • Camphor is a potentially dangerous drug which nevertheless remains popular as a home remedy [1].
  • In this communication, a modulation in oxidation/reduction potential via ligation of substrate and protein components in the camphor 5-exo-monoxygenase system is described in terms of a four-state system using as fundamental parameters the transition free energies between equilibrium states [34].
  • Resonance Raman spectroscopy is applied to the cyanide adducts of cytochrome P450cam and its T252A and D251N site-directed mutants, both in their substrate-free and camphor-bound forms, to probe active-site heme structure and, in particular, interactions of the FeCN fragment with potential active-site H-bond donors [35].
  • Radioimmunoassay results showed that PB P-450 was induced 6-fold by camphor and to a lesser extent by menthol and pinene [36].


  1. Chronic camphor ingestion mimicking Reye's syndrome. Jimenez, J.F., Brown, A.L., Arnold, W.C., Byrne, W.J. Gastroenterology (1983) [Pubmed]
  2. Camphor hydroxylase of Pseudomonas putida: vestiges of sequence homology in cytochrome P-450CAM, putidaredoxin, and related proteins. Dus, K.M. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  3. Putidaredoxin reductase-putidaredoxin-cytochrome p450cam triple fusion protein. Construction of a self-sufficient Escherichia coli catalytic system. Sibbesen, O., De Voss, J.J., Montellano, P.R. J. Biol. Chem. (1996) [Pubmed]
  4. The desymmetrization of bicyclic beta -diketones by an enzymatic retro-Claisen reaction. A new reaction of the crotonase superfamily. Grogan, G., Roberts, G.A., Bougioukou, D., Turner, N.J., Flitsch, S.L. J. Biol. Chem. (2001) [Pubmed]
  5. Lack of regio- and stereospecificity in oxidation of (+) camphor by Streptomyces griseus enriched in cytochrome P-450soy. Sariaslani, F.S., McGee, L.R., Trower, M.K., Kitson, F.G. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  6. Degradation of aqueous solutions of camphor by heterogeneous photocatalysis. Sirtori, C., Altvater, P.K., de Freitas, A.M., Peralta-Zamora, P.G. Journal of hazardous materials. (2006) [Pubmed]
  7. Camphor Poisoning: an evidence-based practice guideline for out-of-hospital management. Manoguerra, A.S., Erdman, A.R., Wax, P.M., Nelson, L.S., Caravati, E.M., Cobaugh, D.J., Chyka, P.A., Olson, K.R., Booze, L.L., Woolf, A.D., Keyes, D.C., Christianson, G., Scharman, E.J., Troutman, W.G. Clinical toxicology (Philadelphia, Pa.) (2006) [Pubmed]
  8. The catalytic pathway of cytochrome p450cam at atomic resolution. Schlichting, I., Berendzen, J., Chu, K., Stock, A.M., Maves, S.A., Benson, D.E., Sweet, R.M., Ringe, D., Petsko, G.A., Sligar, S.G. Science (2000) [Pubmed]
  9. On the bacterial cell cycle: Escherichia coli mutants with altered ploidy. Trun, N.J., Gottesman, S. Genes Dev. (1990) [Pubmed]
  10. Estimating hydration changes upon biomolecular reactions from osmotic stress, high pressure, and preferential hydration experiments. Shimizu, S. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  11. Synthesis and application in asymmetric catalysis of camphor-based pyridine ligands. Chelucci, G. Chemical Society reviews (2006) [Pubmed]
  12. Nucleotide sequence of the Pseudomonas putida cytochrome P-450cam gene and its expression in Escherichia coli. Unger, B.P., Gunsalus, I.C., Sligar, S.G. J. Biol. Chem. (1986) [Pubmed]
  13. Thermodynamic properties of oxidation-reduction reactions of bacterial, microsomal, and mitochondrial cytochromes P-450: an entropy-enthalpy compensation effect. Huang, Y.Y., Hara, T., Sligar, S., Coon, M.J., Kimura, T. Biochemistry (1986) [Pubmed]
  14. P-450 binding to substrates camphor and linalool versus pressure. Marden, M.C., Hoa, G.H. Arch. Biochem. Biophys. (1987) [Pubmed]
  15. Microbial oxidation of adamantanone by Pseudomonas putida carrying the camphor catabolic plasmid. Selifonov, S.A. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
  16. Effects of components of Artemisia annua on coccidia infections in chickens. Allen, P.C., Lydon, J., Danforth, H.D. Poult. Sci. (1997) [Pubmed]
  17. The 2-A crystal structure of 6-oxo camphor hydrolase. New structural diversity in the crotonase superfamily. Whittingham, J.L., Turkenburg, J.P., Verma, C.S., Walsh, M.A., Grogan, G. J. Biol. Chem. (2003) [Pubmed]
  18. Measurements of CO geminate recombination in cytochromes P450 and P420. Tian, W.D., Wells, A.V., Champion, P.M., Di Primo, C., Gerber, N., Sligar, S.G. J. Biol. Chem. (1995) [Pubmed]
  19. Interaction of 5-bromocamphor with cytochrome P-450 cam. Production of 5-ketocamphor from a mixed spin state hemoprotein. Gould, P.V., Gelb, M.H., Sligar, S.G. J. Biol. Chem. (1981) [Pubmed]
  20. Probing the interactions of putidaredoxin with redox partners in camphor P450 5-monooxygenase by mutagenesis of surface residues. Holden, M., Mayhew, M., Bunk, D., Roitberg, A., Vilker, V. J. Biol. Chem. (1997) [Pubmed]
  21. Apparent differential response of nuclear envelope cytochrome P-450 following phenobarbital induction arising from a preferential loss during gradient purification. Clawson, G.A., Moody, D.E., Woo, C.H., Smuckler, E.A. Cancer Res. (1981) [Pubmed]
  22. Conditioned augmentation of natural killer cell activity. Independence from nociceptive effects and dependence on interferon-beta. Solvason, H.B., Ghanta, V.K., Hiramoto, R.N. J. Immunol. (1988) [Pubmed]
  23. Unfolding of the bacterial nucleoid both in vivo and in vitro as a result of exposure to camphor. Harrington, E.W., Trun, N.J. J. Bacteriol. (1997) [Pubmed]
  24. Noncompetitive inhibition by camphor of nicotinic acetylcholine receptors. Park, T.J., Seo, H.K., Kang, B.J., Kim, K.T. Biochem. Pharmacol. (2001) [Pubmed]
  25. The flaming funis. Young, W.W., Dedam, J.P., Conley, S., Wickner, P. Obstetrics and gynecology. (2004) [Pubmed]
  26. Monoterpene synthases from common sage (Salvia officinalis). cDNA isolation, characterization, and functional expression of (+)-sabinene synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase. Wise, M.L., Savage, T.J., Katahira, E., Croteau, R. J. Biol. Chem. (1998) [Pubmed]
  27. Mutagenesis of a single hydrogen bond in cytochrome P-450 alters cation binding and heme solvation. Di Primo, C., Hui Bon Hoa, G., Douzou, P., Sligar, S. J. Biol. Chem. (1990) [Pubmed]
  28. The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450. Poulos, T.L., Finzel, B.C., Gunsalus, I.C., Wagner, G.C., Kraut, J. J. Biol. Chem. (1985) [Pubmed]
  29. Active sites of the cytochrome p450cam (CYP101) F87W and F87A mutants. Evidence for significant structural reorganization without alteration of catalytic regiospecificity. Tuck, S.F., Graham-Lorence, S., Peterson, J.A., Ortiz de Montellano, P.R. J. Biol. Chem. (1993) [Pubmed]
  30. Phenotypic characterization of overexpression or deletion of the Escherichia coli crcA, cspE and crcB genes. Sand, O., Gingras, M., Beck, N., Hall, C., Trun, N. Microbiology (Reading, Engl.) (2003) [Pubmed]
  31. 1-((7,7-Dimethyl-2(S)-(2(S)-amino-4-(methylsulfonyl)butyramido)bicyclo [2.2.1]-heptan-1(S)-yl)methyl)sulfonyl)-4-(2-methylphenyl)piperaz ine (L-368,899): an orally bioavailable, non-peptide oxytocin antagonist with potential utility for managing preterm labor. Williams, P.D., Anderson, P.S., Ball, R.G., Bock, M.G., Carroll, L., Chiu, S.H., Clineschmidt, B.V., Culberson, J.C., Erb, J.M., Evans, B.E. J. Med. Chem. (1994) [Pubmed]
  32. Camphor activates and strongly desensitizes the transient receptor potential vanilloid subtype 1 channel in a vanilloid-independent mechanism. Xu, H., Blair, N.T., Clapham, D.E. J. Neurosci. (2005) [Pubmed]
  33. Camphor intoxication treated by resin hemoperfusion. Kopelman, R., Miller, S., Kelly, R., Sunshine, I. JAMA (1979) [Pubmed]
  34. A thermodynamic model of regulation: modulation of redox equilibria in camphor monoxygenase. Sligar, S.G., Gunsalus, I.C. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
  35. Hydrogen-bonding interactions in the active sites of cytochrome P450cam and its site-directed mutants. Deng , T., Macdonald, I.D., Simianu, M.C., Sykora, M., Kincaid, J.R., Sligar, S.G. J. Am. Chem. Soc. (2001) [Pubmed]
  36. The effect of terpenoid compounds on cytochrome P-450 levels in rat liver. Austin, C.A., Shephard, E.A., Pike, S.F., Rabin, B.R., Phillips, I.R. Biochem. Pharmacol. (1988) [Pubmed]
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