Camphor 5-monooxygenase
Details
- Name
- Camphor 5-monooxygenase
- Synonyms
- 1.14.15.1
- cyp101
- Cytochrome P450-cam
- Cytochrome P450cam
- Gene Name
- camC
- Organism
- Pseudomonas putida
- Amino acid sequence
>lcl|BSEQ0010868|Camphor 5-monooxygenase MTTETIQSNANLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCN GGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQRQFRALANQVV GMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFPIRIFMLLAGLPEEDIPHLKY LTDQMTRPDGSMTFAEAKEALYDYLIPIIEQRRQKPGTDAISIVANGQVNGRPITSDEAK RMCGLLLVGGLDTVVNFLSFSMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGR ILTSDYEFHGVQLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLG QHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPATTKAV
- Number of residues
- 415
- Molecular Weight
- 46668.8
- Theoretical pI
- 5.08
- GO Classification
- Functionscamphor 5-monooxygenase activity / heme binding / iron ion bindingProcesses(+)-camphor catabolic processComponentscytoplasm
- General Function
- Iron ion binding
- Specific Function
- Involved in a camphor oxidation system.
- Pfam Domain Function
- p450 (PF00067)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0002480|1248 bp ATGACGACTGAAACCATACAAAGCAACGCCAATCTTGCCCCTCTGCCACCCCATGTGCCA GAGCACCTGGTATTCGACTTCGACATGTACAATCCGTCGAATCTGTCTGCCGGCGTGCAG GAGGCCTGGGCAGTTCTGCAAGAATCAAACGTACCGGATCTGGTGTGGACTCGCTGCAAC GGCGGACACTGGATCGCCACTCGCGGCCAACTGATCCGTGAGGCCTATGAAGATTACCGC CACTTTTCCAGCGAGTGCCCGTTCATCCCTCGTGAAGCCGGCGAAGCCTACGACTTCATT CCCACCTCGATGGATCCGCCCGAGCAGCGCCAGTTTCGTGCGCTGGCCAACCAAGTGGTT GGCATGCCGGTGGTGGATAAGCTGGAGAACCGGATCCAGGAGCTGGCCTGCTCGCTGATC GAGAGCCTGCGCCCGCAAGGACAGTGCAACTTCACCGAGGACTACGCCGAACCCTTCCCG ATACGCATCTTCATGCTGCTCGCAGGTCTACCGGAAGAAGATATCCCGCACTTGAAATAC CTAACGGATCAGATGACCCGTCCGGATGGCAGCATGACCTTCGCAGAGGCCAAGGAGGCG CTCTACGACTATCTGATACCGATCATCGAGCAACGCAGGCAGAAGCCGGGAACCGACGCT ATCAGCATCGTTGCCAACGGCCAGGTCAATGGGCGACCGATCACCAGTGACGAAGCCAAG AGGATGTGTGGCCTGTTACTGGTCGGCGGCCTGGATACGGTGGTCAATTTCCTCAGCTTC AGCATGGAGTTCCTGGCCAAAAGCCCGGAGCATCGCCAGGAGCTGATCGAGCGTCCCGAG CGTATTCCAGCCGCTTGCGAGGAACTACTCCGGCGCTTCTCGCTGGTTGCCGATGGCCGC ATCCTCACCTCCGATTACGAGTTTCATGGCGTGCAACTGAAGAAAGGTGACCAGATCCTG CTACCGCAGATGCTGTCTGGCCTGGATGAGCGCGAAAACGCCTGCCCGATGCACGTCGAC TTCAGTCGCCAAAAGGTTTCACACACCACCTTTGGCCACGGCAGCCATCTGTGCCTTGGC CAGCACCTGGCCCGCCGGGAAATCATCGTCACCCTCAAGGAATGGCTGACCAGGATTCCT GACTTCTCCATTGCCCCGGGTGCCCAGATTCAGCACAAGAGCGGCATCGTCAGCGGCGTG CAGGCACTCCCTCTGGTCTGGGATCCGGCGACTACCAAAGCGGTATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P00183 UniProtKB Entry Name CPXA_PSEPU GenBank Protein ID 151115 GenBank Gene ID M12546 - General References
- Unger BP, Gunsalus IC, Sligar SG: Nucleotide sequence of the Pseudomonas putida cytochrome P-450cam gene and its expression in Escherichia coli. J Biol Chem. 1986 Jan 25;261(3):1158-63. [Article]
- Koga H, Yamaguchi E, Matsunaga K, Aramaki H, Horiuchi T: Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam hydroxylase of Pseudomonas putida. J Biochem. 1989 Nov;106(5):831-6. [Article]
- Haniu M, Armes LG, Yasunobu KT, Shastry BA, Gunsalus IC: Amino acid sequence of the Pseudomonas putida cytochrome P-450. II. Cyanogen bromide peptides, acid cleavage peptides, and the complete sequence. J Biol Chem. 1982 Nov 10;257(21):12664-71. [Article]
- Marden MC, Hoa GH: P-450 binding to substrates camphor and linalool versus pressure. Arch Biochem Biophys. 1987 Feb 15;253(1):100-7. [Article]
- Hui Bon Hoa G, Di Primo C, Dondaine I, Sligar SG, Gunsalus IC, Douzou P: Conformational changes of cytochromes P-450cam and P-450lin induced by high pressure. Biochemistry. 1989 Jan 24;28(2):651-6. [Article]
- Nolting B, Jung C, Snatzke G: Multichannel circular dichroism investigations of the structural stability of bacterial cytochrome P-450. Biochim Biophys Acta. 1992 May 20;1100(2):171-6. [Article]
- Deprez E, Gill E, Helms V, Wade RC, Hui Bon Hoa G: Specific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin. J Inorg Biochem. 2002 Sep 20;91(4):597-606. [Article]
- Poulos TL, Finzel BC, Gunsalus IC, Wagner GC, Kraut J: The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450. J Biol Chem. 1985 Dec 25;260(30):16122-30. [Article]
- Schlichting I, Jung C, Schulze H: Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer. FEBS Lett. 1997 Oct 6;415(3):253-7. [Article]
- Vidakovic M, Sligar SG, Li H, Poulos TL: Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect. Biochemistry. 1998 Jun 30;37(26):9211-9. [Article]
- Dmochowski IJ, Crane BR, Wilker JJ, Winkler JR, Gray HB: Optical detection of cytochrome P450 by sensitizer-linked substrates. Proc Natl Acad Sci U S A. 1999 Nov 9;96(23):12987-90. [Article]
- Schlichting I, Berendzen J, Chu K, Stock AM, Maves SA, Benson DE, Sweet RM, Ringe D, Petsko GA, Sligar SG: The catalytic pathway of cytochrome p450cam at atomic resolution. Science. 2000 Mar 3;287(5458):1615-22. [Article]
- Hishiki T, Shimada H, Nagano S, Egawa T, Kanamori Y, Makino R, Park SY, Adachi S, Shiro Y, Ishimura Y: X-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome P450cam: roles of Thr252 and water in the active center. J Biochem. 2000 Dec;128(6):965-74. [Article]
- Lee DS, Park SY, Yamane K, Obayashi E, Hori H, Shiro Y: Structural characterization of n-butyl-isocyanide complexes of cytochromes P450nor and P450cam. Biochemistry. 2001 Mar 6;40(9):2669-77. [Article]
- Dunn AR, Dmochowski IJ, Bilwes AM, Gray HB, Crane BR: Probing the open state of cytochrome P450cam with ruthenium-linker substrates. Proc Natl Acad Sci U S A. 2001 Oct 23;98(22):12420-5. Epub 2001 Oct 16. [Article]
- Fedorov R, Ghosh DK, Schlichting I: Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes. Arch Biochem Biophys. 2003 Jan 1;409(1):25-31. [Article]
- Mouro C, Bondon A, Simonneaux G, Jung C: 1H-NMR study of diamagnetic cytochrome P450cam: assignment of heme resonances and substrate dependance of one cysteinate beta proton. FEBS Lett. 1997 Sep 8;414(2):203-8. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01663 lambda-bis(2,2'-bipyridine)-(5-methyl-2-2'-bipyridine)-C9-adamantane ruthenium (II) experimental unknown Details DB01703 N-(2-ferrocenylethyl)maleimide experimental unknown Details DB01744 Camphor approved, withdrawn unknown substrate Details DB01826 N-Butyl Isocyanide experimental unknown Details DB01011 Metyrapone approved, investigational unknown other/unknown Details DB02125 Adamantanone experimental unknown Details DB02617 1-(N-Imidazolyl)-2-Hydroxy-2-(2,3-Dichlorophenyl)Octane experimental unknown Details DB02817 5-Exo-Hydroxycamphor experimental unknown Details DB02851 Thiocamphor experimental unknown Details DB03031 Adamantane-1-Carboxylic Acid-5-Dimethylamino-Naphthalene-1-Sulfonylamino-Octyl-Amide experimental unknown Details DB03540 Norcamphor experimental unknown Details DB03627 Adamantane experimental unknown Details DB03836 1,3,5-trichlorobenzene experimental unknown Details DB04032 Adamantane-1-Carboxylic Acid-5-Dimethylamino-Naphthalene-1-Sulfonylamino-Butyl-Amide experimental unknown Details DB04501 Camphane experimental unknown Details