Camphor 5-monooxygenase

NameCamphor 5-monooxygenase
Synonyms
  • 1.14.15.1
  • cyp101
  • Cytochrome P450-cam
  • Cytochrome P450cam
Gene NamecamC
OrganismPseudomonas putida
Amino acid sequence
>lcl|BSEQ0010868|Camphor 5-monooxygenase
MTTETIQSNANLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCN
GGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQRQFRALANQVV
GMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFPIRIFMLLAGLPEEDIPHLKY
LTDQMTRPDGSMTFAEAKEALYDYLIPIIEQRRQKPGTDAISIVANGQVNGRPITSDEAK
RMCGLLLVGGLDTVVNFLSFSMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGR
ILTSDYEFHGVQLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLG
QHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPATTKAV
Number of residues415
Molecular Weight46668.8
Theoretical pI5.08
GO Classification
Functions
  • iron ion binding
  • heme binding
  • camphor 5-monooxygenase activity
Processes
  • (+)-camphor catabolic process
Components
  • cytoplasm
General FunctionIron ion binding
Specific FunctionInvolved in a camphor oxidation system.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID151115
UniProtKB IDP00183
UniProtKB Entry NameCPXA_PSEPU
Cellular LocationCytoplasm
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
GenBank Gene IDM12546
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
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. 3003058
  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. 2613690
  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. 7130171
  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. 3813557
  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. 2578028
  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. 1610873
  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. 12237225
  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. 4066706
  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. 9357977
  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. 9649301
  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. 10557259
  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. 10698731
  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. 11098139
  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. 11258878
  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. 11606730
  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. 12464241
  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. 9315686