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
Functions
camphor 5-monooxygenase activity / heme binding / iron ion binding
Processes
(+)-camphor catabolic process
Components
cytoplasm
General Function
Iron ion binding
Specific Function
Involved in a camphor oxidation system.
Pfam Domain Function
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
ResourceLink
UniProtKB IDP00183
UniProtKB Entry NameCPXA_PSEPU
GenBank Protein ID151115
GenBank Gene IDM12546
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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]
  17. 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 IDNameDrug groupPharmacological action?ActionsDetails
DB01663lambda-bis(2,2'-bipyridine)-(5-methyl-2-2'-bipyridine)-C9-adamantane ruthenium (II)experimentalunknownDetails
DB01703N-(2-ferrocenylethyl)maleimideexperimentalunknownDetails
DB01744Camphorapproved, withdrawnunknownsubstrateDetails
DB01826N-Butyl IsocyanideexperimentalunknownDetails
DB01011Metyraponeapproved, investigationalunknownother/unknownDetails
DB02125AdamantanoneexperimentalunknownDetails
DB026171-(N-Imidazolyl)-2-Hydroxy-2-(2,3-Dichlorophenyl)OctaneexperimentalunknownDetails
DB028175-Exo-HydroxycamphorexperimentalunknownDetails
DB02851ThiocamphorexperimentalunknownDetails
DB03031Adamantane-1-Carboxylic Acid-5-Dimethylamino-Naphthalene-1-Sulfonylamino-Octyl-AmideexperimentalunknownDetails
DB03540NorcamphorexperimentalunknownDetails
DB03627AdamantaneexperimentalunknownDetails
DB038361,3,5-trichlorobenzeneexperimentalunknownDetails
DB04032Adamantane-1-Carboxylic Acid-5-Dimethylamino-Naphthalene-1-Sulfonylamino-Butyl-AmideexperimentalunknownDetails
DB04501CamphaneexperimentalunknownDetails