EzCatDB: S00033

DB codeS00033
RLCP classification10.21100.110.10515
CATH domainDomain 11.10.630.10Catalytic domain
E.C.1.14.15.1
CSA1akd
MACiEM0133

CATH domainRelated DB codes (homologues)
1.10.630.10S00031,M00154,S00030

Enzyme Name
Swiss-protKEGG

P00183
Protein nameCamphor 5-monooxygenasecamphor 5-monooxygenase
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
camphor methylene hydroxylase
SynonymsEC 1.14.15.1
Cytochrome P450-cam
P450cam


Swiss-prot:Accession NumberP00183
Entry nameCPXA_PSEPU
Activity(+)-camphor + putidaredoxin + O(2) = (+)-exo- 5-hydroxycamphor + oxidized putidaredoxin + H(2)O.
Subunit
Subcellular locationCytoplasm (By similarity).
CofactorHeme group.


CofactorsSubstratesProductsintermediates
KEGG-idC00032C00808C02069C00007C03448C03302C00001



CompoundHeme(+)-CamphorPutidaredoxinO2(+)-exo-5-HydroxycamphorOxidized putidaredoxinH2OFeIII-O-O FeIII-O-O FeIII-O-OH FeIV=O
Typearomatic ring (with nitrogen atoms),carboxyl group,heavy metalcarbohydrateheavy metal,peptide/protein,sulfide groupotherscarbohydrateheavy metal,peptide/protein,sulfide groupH2O



1akdABound:HEMBound:CAMUnboundUnboundUnboundUnbound




1c8jABound:HEMUnboundUnboundUnboundUnboundUnbound




1c8jBBound:HEMUnboundUnboundUnboundUnboundUnbound




1cp4AAnalogue:HEM-BNZUnboundUnboundUnboundUnboundUnbound




1dz4ABound:HEMBound:CAMUnboundUnboundUnboundUnbound




1dz4BBound:HEMBound:CAMUnboundUnboundUnboundUnbound




1dz6ABound:HEMBound:CAMUnboundUnboundUnboundUnbound




1dz6BBound:HEMBound:CAMUnboundUnboundUnboundUnbound




1dz8ABound:HEMBound:CAMUnboundBound:OXYUnboundUnbound




1dz8BBound:HEMBound:CAMUnboundUnboundUnboundUnbound




1dz9ABound:HEMBound:CAMUnboundUnboundUnboundUnbound



Bound:__O
1dz9BBound:HEMBound:CAMUnboundUnboundUnboundUnbound



Unbound
1gebABound:HEMBound:CAMUnboundUnboundUnboundUnbound




1gekAAnalogue:HEM-NBNUnboundUnboundUnboundUnboundUnbound




1gemAAnalogue:HEM-NBNUnboundUnboundUnboundUnboundUnbound




1gjmABound:HEMUnboundUnboundUnboundUnboundUnbound




1iwiABound:HEMBound:CAMUnboundUnboundUnboundUnbound




1iwjABound:HEMBound:CAMUnboundUnboundUnboundUnbound




1iwkABound:HEMUnboundUnboundUnboundUnboundUnbound




1j51ABound:HEMAnalogue:TCZUnboundUnboundUnboundUnbound




1j51BBound:HEMAnalogue:TCZUnboundUnboundUnboundUnbound




1j51CBound:HEMAnalogue:TCZUnboundUnboundUnboundUnbound




1j51DBound:HEMUnboundUnboundUnboundUnboundUnbound




1k2oABound:HEMAnalogue:RFA-RFBUnboundUnboundUnboundUnbound




1k2oBBound:HEMAnalogue:RFA-RFBUnboundUnboundUnboundUnbound




1lwlABound:HEMAnalogue:DSOUnboundUnboundUnboundUnbound




1mpwABound:HEMUnboundUnboundUnboundAnalogue:TMHUnbound




1mpwBBound:HEMUnboundUnboundUnboundAnalogue:TMHUnbound




1nooABound:HEMUnboundUnboundUnboundBound:CAHUnbound




1o76ABound:HEMBound:CAMUnboundAnalogue:CYNUnboundUnbound




1o76BBound:HEMBound:CAMUnboundAnalogue:CYNUnboundUnbound




1p2yAAnalogue:HEM-NCTUnboundUnboundUnboundUnboundUnbound




1p7rABound:HEMAnalogue:NCTUnboundUnboundUnboundUnbound




1phaAAnalogue:HEM-PFZUnboundUnboundUnboundUnboundUnbound




1phbAAnalogue:HEM-PFZUnboundUnboundUnboundUnboundUnbound




1phcABound:HEMUnboundUnboundUnboundUnboundUnbound




1phdAAnalogue:HEM-PIMUnboundUnboundUnboundUnboundUnbound




1pheABound:HEMAnalogue:PIMUnboundUnboundUnboundUnbound



Analogue:SO4
1phfAAnalogue:HEM-PIMUnboundUnboundUnboundUnboundUnbound




1phgAAnalogue:HEM-MYTUnboundUnboundUnboundUnboundUnbound




1qmqABound:HEMAnalogue:LRB-DRBUnboundUnboundUnboundUnbound




1re9ABound:HEMAnalogue:DSOUnboundUnboundUnboundUnbound




1rf9ABound:HEMAnalogue:DBRUnboundUnboundUnboundUnbound




1t85ABound:HEMBound:CAMUnboundAnalogue:CMOUnboundUnbound




1t86ABound:HEMBound:CAMUnboundUnboundUnboundUnbound




1t86BBound:HEMBound:CAMUnboundUnboundUnboundUnbound




1t87ABound:HEMBound:CAMUnboundUnboundUnboundUnbound




1t87BBound:HEMBound:CAMUnboundAnalogue:CMOUnboundUnbound




1t88ABound:HEMBound:CAMUnboundUnboundUnboundUnbound




1t88BBound:HEMBound:CAMUnboundUnboundUnboundUnbound




1uyuABound:HEMBound:CAMUnboundUnboundUnboundUnbound




1uyuBBound:HEMBound:CAMUnboundUnboundUnboundUnbound




1yrcABound:HEMBound:CAMUnboundUnboundUnboundUnbound




1yrdABound:HEMBound:CAMUnboundUnboundUnboundUnbound




2a1mABound:HEMBound:CAMUnboundBound:OXYUnboundUnbound




2a1mBBound:HEMBound:CAMUnboundBound:OXYUnboundUnbound




2a1nABound:HEMBound:CAMUnboundBound:OXYUnboundUnbound




2a1nBBound:HEMBound:CAMUnboundBound:OXYUnboundUnbound




2a1oABound:HEMBound:CAMUnboundBound:OXYUnboundUnbound




2a1oBBound:HEMBound:CAMUnboundBound:OXYUnboundUnbound




2cp4ABound:HEMBound:CAMUnboundUnboundUnboundUnbound




2cppABound:HEMBound:CAMUnboundUnboundUnboundUnbound




2fe6AAnalogue:MNRUnboundUnboundUnboundUnboundUnbound




2ferAAnalogue:MNRUnboundUnboundUnboundUnboundUnbound




2feuAAnalogue:MNRBound:CAMUnboundUnboundUnboundUnbound




2feuBAnalogue:MNRBound:CAMUnboundUnboundUnboundUnbound




2frzABound:HEMUnboundUnboundUnboundUnboundUnbound




2frzBBound:HEMUnboundUnboundUnboundUnboundUnbound




2gqxABound:HEMAnalogue:5CLUnboundUnboundUnboundUnbound




2gqxBBound:HEMUnboundUnboundUnboundUnboundUnbound




2gr6ABound:HEMUnboundUnboundUnboundUnboundUnbound




2gr6BBound:HEMUnboundUnboundUnboundUnboundUnbound




2h7qAAnalogue:HEM-IMDUnboundUnboundUnboundUnboundUnbound




2h7rAAnalogue:HEM-1MZUnboundUnboundUnboundUnboundUnbound




2h7sABound:HEMUnboundUnboundUnboundUnboundUnbound




2h7sCBound:HEMUnboundUnboundUnboundUnboundUnbound




2qblABound:HEMBound:CAMUnboundUnboundUnboundUnbound




2qbmABound:HEMBound:CAMUnboundAnalogue:CYNUnboundUnbound




2qbnABound:HEMBound:CAMUnboundUnboundUnboundUnbound




2qboABound:HEMBound:CAMUnboundAnalogue:CYNUnboundUnbound




2zawAAnalogue:6HEBound:CAMUnboundUnboundUnboundUnbound




2zaxABound:HEMBound:CAMUnboundUnboundUnboundUnbound




3cp4ABound:HEMAnalogue:ADMUnboundUnboundUnboundUnbound




3cppABound:HEMBound:CAMUnboundAnalogue:CMOUnboundUnbound




4cp4ABound:HEMBound:CAMUnboundUnboundUnboundUnbound




4cppABound:HEMAnalogue:ADMUnboundUnboundUnboundUnbound




5cp4ABound:HEMBound:CAMUnboundUnboundUnboundUnbound




5cppABound:HEMAnalogue:ADOUnboundUnboundUnboundUnbound




6cp4ABound:HEMBound:CAMUnboundUnboundUnboundUnbound




6cppABound:HEMAnalogue:CAEUnboundUnboundUnboundUnbound




7cppABound:HEMAnalogue:NCMUnboundUnboundUnboundUnbound




8cppABound:HEMUnboundUnboundUnboundAnalogue:TCMUnbound





Active-site residues
resource
literature [9], [11], [30], [37]
pdbCatalytic residuesCofactor-binding residuescomment
1akdAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1c8jAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant F87W, Y96F
1c8jBARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant F87W, Y96F
1cp4AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1dz4AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1dz4BARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1dz6AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1dz6BARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1dz8AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1dz8BARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1dz9AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1dz9BARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1gebAARG 112;LYS 178;ARG 186;ASP 251;       
CYS 357(Iron binding)
mutant T252I
1gekAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1gemAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1gjmAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1iwiAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1iwjAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant R109K
1iwkA       ;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant R112K
1j51AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant F87Y, Y96F, V247L, C334A
1j51BARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant F87Y, Y96F, V247L, C334A
1j51CARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant F87Y, Y96F, V247L, C334A
1j51DARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant F87Y, Y96F, V247L, C334A
1k2oAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutation C334A
1k2oBARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutation C334A
1lwlAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1mpwAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant F87W, Y96F, V247L, C334A
1mpwBARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant F87W, Y96F, V247L, C334A
1nooAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1o76AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1o76BARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1p2yAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1p7rAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1phaAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1phbAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1phcAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1phdAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1pheAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1phfAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1phgAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1qmqAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant C334A
1re9AARG 102;LYS 168;ARG 176;ASP 241;THR 242
CYS 347(Iron binding)

1rf9AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1t85AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant C334A, L358P
1t86AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant C334A, L358P
1t86BARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant C334A, L358P
1t87AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant C334A
1t87BARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant C334A
1t88AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant C334A
1t88BARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant C334A
1uyuAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1uyuBARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1yrcAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

1yrdAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

2a1mAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

2a1mBARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

2a1nAARG 112;LYS 178;ARG 186;       ;THR 252
CYS 357(Iron binding)
mutant D251N
2a1nBARG 112;LYS 178;ARG 186;       ;THR 252
CYS 357(Iron binding)
mutant D251N
2a1oAARG 112;LYS 178;ARG 186;ASP 251;       
CYS 357(Iron binding)
mutant T252A
2a1oBARG 112;LYS 178;ARG 186;ASP 251;       
CYS 357(Iron binding)
mutant T252A
2cp4AARG 112;LYS 178;ARG 186;ASP 251;       
CYS 357(Iron binding)
mutant T252A
2cppAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

2fe6AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

2ferAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

2feuAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

2feuBARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

2frzAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant F87W, Y96F, V247L, C334A
2frzBARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant F87W, Y96F, V247L, C334A
2gqxAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant F87W, Y96F, L244A, V247L, C334A
2gqxBARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant F87W, Y96F, L244A, V247L, C334A
2gr6AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant F87W, Y96F, L244A, V247L, C334A
2gr6BARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant F87W, Y96F, L244A, V247L, C334A
2h7qAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

2h7rAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant L244A
2h7sAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant L244A
2h7sCARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant L244A
2qblAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant G248T
2qbmAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant G248T
2qbnAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant G248V
2qboAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)
mutant G248V
2zawAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

2zaxAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

3cp4AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

3cppAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

4cp4AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

4cppAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

5cp4AARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

5cppAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

6cp4AARG 112;LYS 178;ARG 186;       ;THR 252
CYS 357(Iron binding)
mutant D251N
6cppAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

7cppAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)

8cppAARG 112;LYS 178;ARG 186;ASP 251;THR 252
CYS 357(Iron binding)


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.16129
[8]p.7590-7591
[11]Fig.1, p.11426-11428
[12]p.2680
[17]Fig.1, Fig.3, p.677-678
[21]Fig.1, p.1179-1182
[25]Fig.10, p.1076
[30]p.9216-9218, Fig.10
[31]p.166
[32]Fig.1, p.176-177
[37]p.972-973, Fig.6
[40]

[41]Fig.1, p.1617-1621
[42]Fig.1
[52]p.14512-14513
[54]Fig.4
[55]p.31662-31663
[58]Fig.1, p.508-514
[60]Scheme 1, p.477-479
[61]Fig.1, p.14136-14139

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID86059514
PubMed ID4066706
JournalJ Biol Chem
Year1985
Volume260
Pages16122-30
AuthorsPoulos TL, Finzel BC, Gunsalus IC, Wagner GC, Kraut J
TitleThe 2.6-A crystal structure of Pseudomonas putida cytochrome P-450.
Related Swiss-protP00183
[2]
CommentsX-ray crystallography
PubMed ID3768350
JournalBiochemistry
Year1986
Volume25
Pages5314-22
AuthorsPoulos TL, Finzel BC, Howard AJ
TitleCrystal structure of substrate-free Pseudomonas putida cytochrome P-450.
Related PDB1phc
[3]
CommentsABSORPTION SPECTROSCOPY
Medline ID87126838
PubMed ID3813557
JournalArch Biochem Biophys
Year1987
Volume253
Pages100-7
AuthorsMarden MC, Hoa GH
TitleP-450 binding to substrates camphor and linalool versus pressure.
Related Swiss-protP00183
[4]
CommentsX-ray crystallography
PubMed ID3442650
JournalBiochemistry
Year1987
Volume26
Pages8165-74
AuthorsPoulos TL, Howard AJ
TitleCrystal structures of metyrapone- and phenylimidazole-inhibited complexes of cytochrome P-450cam.
Related PDB1phd,1phe,1phf,1phg
[5]
CommentsX-ray crystallography
PubMed ID3656428
JournalJ Mol Biol
Year1987
Volume195
Pages687-700
AuthorsPoulos TL, Finzel BC, Howard AJ
TitleHigh-resolution crystal structure of cytochrome P450cam.
Related PDB1noo,2cpp
[6]
CommentsFOURIER-TRANSFORM INFRARED SPECTROSCOPY
JournalStud Biophys
Year1987
Volume120
Pages241-51
AuthorsJung C, Marlow F
TitleDynamic behavior of the active site structure in bacterial cytochrome P-450.
Related Swiss-protP00183
[7]
CommentsABSORPTION AND FLUORESCENCE SPECTROSCOPY
Medline ID89229061
PubMed ID2578028
JournalBiochemistry
Year1989
Volume28
Pages651-6
AuthorsHui Bon Hoa G, Di Primo C, Dondaine I, Sligar SG, Gunsalus IC, Douzou P
TitleConformational changes of cytochromes P-450cam and P-450lin induced by high pressure.
Related Swiss-protP00183
[8]
CommentsX-ray crystallography
PubMed ID2611203
JournalBiochemistry
Year1989
Volume28
Pages7586-92
AuthorsRaag R, Poulos TL
TitleCrystal structure of the carbon monoxide-substrate-cytochrome P-450CAM ternary complex.
Related PDB3cpp
[9]
CommentsX-ray crystallography
PubMed ID2713354
JournalBiochemistry
Year1989
Volume28
Pages917-22
AuthorsRaag R, Poulos TL
TitleThe structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM.
Related PDB5cpp,7cpp
[10]
CommentsX-ray crystallography
PubMed ID2261467
JournalBiochemistry
Year1990
Volume29
Pages8119-26
AuthorsRaag R, Swanson BA, Poulos TL, Ortiz de Montellano PR
TitleFormation, crystal structure, and rearrangement of a cytochrome P-450cam iron-phenyl complex.
Related PDB1cp4
[11]
CommentsX-ray crystallography
PubMed ID1742281
JournalBiochemistry
Year1991
Volume30
Pages11420-9
AuthorsRaag R, Martinis SA, Sligar SG, Poulos TL
TitleCrystal structure of the cytochrome P-450CAM active site mutant Thr252Ala.
Related PDB2cp4,3cp4,4cp4
[12]
CommentsX-ray crystallography
PubMed ID2001355
JournalBiochemistry
Year1991
Volume30
Pages2674-84
AuthorsRaag R, Poulos TL
TitleCrystal structures of cytochrome P-450CAM complexed with camphane, thiocamphor, and adamantane: factors controlling P-450 substrate hydroxylation.
Related PDB4cpp,6cpp,8cpp
[13]
PubMed ID1764462
JournalBiochim Biophys Acta
Year1991
Volume1115
Pages101-7
AuthorsShiro Y, Makino R, Sato F, Oyanagi H, Matsushita T, Ishimura Y, Iizuka T
TitleStructural and electronic characterization of heme moiety in oxygenated hemoproteins by using XANES spectroscopy.
[14]
PubMed ID1749772
JournalProteins
Year1991
Volume11
Pages184-204
AuthorsPaulsen MD, Ornstein RL
TitleA 175-psec molecular dynamics simulation of camphor-bound cytochrome P-450cam.
[15]
PubMed ID1449498
JournalBiochem Biophys Res Commun
Year1992
Volume189
Pages488-95
AuthorsFilipovic D, Paulsen MD, Loida PJ, Sligar SG, Ornstein RL
TitleEthylbenzene hydroxylation by cytochrome P450cam.
[16]
CommentsCIRCULAR DICHROISM SPECTROSCOPY
Medline ID92305023
PubMed ID1610873
JournalBiochim Biophys Acta
Year1992
Volume1100
Pages171-6
AuthorsNolting B, Jung C, Snatzke G
TitleMultichannel circular dichroism investigations of the structural stability of bacterial cytochrome P-450.
Related Swiss-protP00183
[17]
PubMed ID1537455
JournalFASEB J
Year1992
Volume6
Pages674-9
AuthorsPoulos TL, Raag R
TitleCytochrome P450cam: crystallography, oxygen activation, and electron transfer.
[18]
CommentsX-ray crystallography
PubMed ID8485133
JournalBiochemistry
Year1993
Volume32
Pages4571-8
AuthorsRaag R, Li H, Jones BC, Poulos TL
TitleInhibitor-induced conformational change in cytochrome P-450CAM.
Related PDB1pha,1phb
[19]
PubMed ID8332592
JournalProtein Eng
Year1993
Volume6
Pages359-65
AuthorsPaulsen MD, Ornstein RL
TitleSubstrate mobility in thiocamphor-bound cytochrome P450cam: an explanation of the conflict between the observed product profile and the X-ray structure.
[20]
PubMed ID8034004
JournalFEBS Lett
Year1994
Volume347
Pages207-10
AuthorsDeprez E, Di Primo C, Hoa GH, Douzou P
TitleEffects of monovalent cations on cytochrome P-450 camphor. Evidence for preferential binding of potassium.
[21]
PubMed ID8120894
JournalJ Mol Biol
Year1994
Volume236
Pages1169-85
AuthorsHasemann CA, Ravichandran KG, Peterson JA, Deisenhofer J
TitleCrystal structure and refinement of cytochrome P450terp at 2.3 A resolution.
[22]
PubMed ID7700866
JournalProtein Eng
Year1994
Volume7
Pages1345-51
AuthorsRuan KH, Milfeld K, Kulmacz RJ, Wu KK
TitleComparison of the construction of a 3-D model for human thromboxane synthase using P450cam and BM-3 as templates: implications for the substrate binding pocket.
[23]
PubMed ID8519982
JournalBiophys J
Year1995
Volume69
Pages810-24
AuthorsHelms V, Wade RC
TitleThermodynamics of water mediating protein-ligand interactions in cytochrome P450cam: a molecular dynamics study.
[24]
PubMed ID8637849
JournalProtein Eng
Year1995
Volume8
Pages801-7
AuthorsManchester JI, Ornstein RL
TitleEnzyme-catalyzed dehalogenation of pentachloroethane: why F87W-cytochrome P450cam is faster than wild type.
[25]
PubMed ID7549871
JournalProtein Sci
Year1995
Volume4
Pages1065-80
AuthorsGraham-Lorence S, Amarneh B, White RE, Peterson JA, Simpson ER
TitleA three-dimensional model of aromatase cytochrome P450.
[26]
CommentsSTRUCTURE BY NMR
Medline ID97459726
PubMed ID9315686
JournalFEBS Lett
Year1997
Volume414
Pages203-8
AuthorsMouro C, Bondon A, Simonneaux G, Jung C
Title1H-NMR study of diamagnetic cytochrome P450cam: assignment of heme resonances and substrate dependance of one cysteinate beta proton.
Related Swiss-protP00183
[27]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID98019009
PubMed ID9357977
JournalFEBS Lett
Year1997
Volume415
Pages253-7
AuthorsSchlichting I, Jung C, Schulze H
TitleCrystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer.
Related PDB1akd
Related Swiss-protP00183
[28]
PubMed ID9122160
JournalProc Natl Acad Sci U S A
Year1997
Volume94
Pages2133-8
AuthorsOprea TI, Hummer G, Garcia AE
TitleIdentification of a functional water channel in cytochrome P450 enzymes.
[29]
PubMed ID9761931
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages470-2
AuthorsNickerson D, Wong LL, Rao Z
TitleAn improved procedure for the preparation of X-ray diffraction-quality crystals of cytochrome p450cam.
[30]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
Medline ID98313255
PubMed ID9649301
JournalBiochemistry
Year1998
Volume37
Pages9211-9
AuthorsVidakovic M, Sligar SG, Li H, Poulos TL
TitleUnderstanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect.
Related PDB5cp4,6cp4
Related Swiss-protP00183
[31]
PubMed ID9675266
JournalBiochim Biophys Acta
Year1998
Volume1386
Pages157-67
AuthorsAoki M, Ishimori K, Morishima I
TitleRoles of negatively charged surface residues of putidaredoxin in interactions with redox partners in p450cam monooxygenase system.
[32]
PubMed ID9675270
JournalBiochim Biophys Acta
Year1998
Volume1386
Pages168-78
AuthorsAoki M, Ishimori K, Morishima I
TitleNMR studies of putidaredoxin: associations of putidaredoxin with NADH-putidaredoxin reductase and cytochrome p450cam.
[33]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
JournalJ Am Chem Soc
Year1998
Volume120
Pages46-52
AuthorsDi Gleria K., Nickerson DP, Hill HAO, Wong LL., Fueloep V
TitleCovalent attachment of an electroactive sulfydryl reagent in the active site of cytochrome P450cam as revealed by the crystal structure of the modified protein.
Related PDB1gjm
Related Swiss-protP00183
[34]
PubMed ID9888815
JournalBiochemistry
Year1999
Volume38
Pages751-61
AuthorsDavydov DR, Hui Bon Hoa G, Peterson JA
TitleDynamics of protein-bound water in the heme domain of P450BM3 studied by high-pressure spectroscopy: comparison with P450cam and P450 2B4.
[35]
CommentsX-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS)
Medline ID20027486
PubMed ID10557259
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages12987-90
AuthorsDmochowski IJ, Crane BR, Wilker JJ, Winkler JR, Gray HB
TitleOptical detection of cytochrome P450 by sensitizer-linked substrates.
Related PDB1qmq
Related Swiss-protP00183
[36]
PubMed ID10601869
JournalEur J Biochem
Year2000
Volume267
Pages216-21
AuthorsMouro C, Bondon A, Jung C, De Certaines JD, Simonneaux G
TitleAssignment of heme methyl 1H-NMR resonances of high-spin and low-spin ferric complexes of cytochrome p450cam using one-dimensional and two-dimensional paramagnetic signals enhancement (PASE) magnetization transfer experiments.
[37]
CommentsX-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS)
Medline ID21062556
PubMed ID11098139
JournalJ Biochem (Tokyo)
Year2000
Volume128
Pages965-74
AuthorsHishiki T, Shimada H, Nagano S, Egawa T, Kanamori Y, Makino R, Park SY, Adachi S, Shiro Y, Ishimura Y
TitleX-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome P450cam: roles of Thr252 and water in the active center.
Related PDB1geb
Related Swiss-protP00183
[38]
PubMed ID11051557
JournalJ Inorg Biochem
Year2000
Volume81
Pages121-31
AuthorsDas B, Helms V, Lounnas V, Wade RC
TitleMulticopy molecular dynamics simulations suggest how to reconcile crystallographic and product formation data for camphor enantiomers bound to cytochrome P-450cam.
[39]
PubMed ID11051567
JournalJ Inorg Biochem
Year2000
Volume81
Pages221-8
AuthorsDmochowski IJ, Winkler JR, Gray HB
TitleEnantiomeric discrimination of Ru-substrates by cytochrome P450cam.
[40]
PubMed ID10742167
JournalNat Struct Biol
Year2000
Volume7
Pages270
AuthorsFeng HP
TitlePicture story. Freeze frame.
[41]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
Medline ID20165028
PubMed ID10698731
JournalScience
Year2000
Volume287
Pages1615-22
AuthorsSchlichting I, Berendzen J, Chu K, Stock AM, Maves SA, Benson DE, Sweet RM, Ringe D, Petsko GA, Sligar SG
TitleThe catalytic pathway of cytochrome p450cam at atomic resolution.
Related PDB1dz4,1dz6,1dz8,1dz9
Related Swiss-protP00183
[42]
PubMed ID11583152
JournalBiochemistry
Year2001
Volume40
Pages9532-8
AuthorsFrench KJ, Strickler MD, Rock DA, Rock DA, Bennett GA, Wahlstrom JL, Goldstein BM, Jones JP
TitleBenign synthesis of 2-ethylhexanoic acid by cytochrome P450cam: enzymatic, crystallographic, and theoretical studies.
[43]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS)
Medline ID21159060
PubMed ID11258878
JournalBiochemistry
Year2001
Volume40
Pages2669-77
AuthorsLee DS, Park SY, Yamane K, Obayashi E, Hori H, Shiro Y
TitleStructural characterization of n-butyl-isocyanide complexes of cytochromes P450nor and P450cam.
Related PDB1gek,1gem
Related Swiss-protP00183
[44]
PubMed ID11688945
JournalJ Comput Aided Mol Des
Year2001
Volume15
Pages649-57
AuthorsKeseru GM
TitleA virtual high throughput screen for high affinity cytochrome P450cam substrates. Implications for in silico prediction of drug metabolism.
[45]
CommentsX-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS)
Medline ID21532932
PubMed ID11606730
JournalProc Natl Acad Sci U S A
Year2001
Volume98
Pages12420-5
AuthorsDunn AR, Dmochowski IJ, Bilwes AM, Gray HB, Crane BR
TitleProbing the open state of cytochrome P450cam with ruthenium-linker substrates.
Related PDB1k2o
Related Swiss-protP00183
[46]
CommentsX-ray crystallography
PubMed ID12197708
JournalJ Am Chem Soc
Year2002
Volume124
Pages10254-5
AuthorsDunn AR, Hays AM, Goodin DB, Stout CD, Chiu R, Winkler JR, Gray HB
TitleFluorescent probes for cytochrome p450 structural characterization and inhibitor screening.
Related PDB1lwl
[47]
CommentsX-ray crystallography
PubMed ID12114516
JournalJ Biol Chem
Year2002
Volume277
Pages37519-26
AuthorsChen X, Christopher A, Jones JP, Bell SG, Guo Q, Xu F, Rao Z, Wong LL
TitleCrystal structure of the F87W/Y96F/V247L mutant of cytochrome P-450cam with 1,3,5-trichlorobenzene bound and further protein engineering for the oxidation of pentachlorobenzene and hexachlorobenzene.
Related PDB1j51
[48]
CommentsSUBSTRATE-PROTEIN INTERACTION
Medline ID22222631
PubMed ID12237225
JournalJ Inorg Biochem
Year2002
Volume91
Pages597-606
AuthorsDeprez E, Gill E, Helms V, Wade RC, Hui Bon Hoa G
TitleSpecific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin.
Related Swiss-protP00183
[49]
PubMed ID12211002
JournalProteins
Year2002
Volume49
Pages216-31
AuthorsKirton SB, Kemp CA, Tomkinson NP, St-Gallay S, Sutcliffe MJ
TitleImpact of incorporating the 2C5 crystal structure into comparative models of cytochrome P450 2D6.
[50]
CommentsX-ray crystallography
JournalArch Biochem Biophys
Year2003
Volume409
Pages25-31
AuthorsFedorov R, Ghosh DK, Schlichting I
TitleCrystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes.
Related PDB1o76
[51]
CommentsX-ray crystallography
PubMed ID14556625
JournalBiochemistry
Year2003
Volume42
Pages11943-50
AuthorsStrickler M, Goldstein BM, Maxfield K, Shireman L, Kim G, Matteson DS, Jones JP
TitleCrystallographic studies on the complex behavior of nicotine binding to P450cam (CYP101).
Related PDB1p2y,1p7r
[52]
CommentsX-ray crystallography
PubMed ID14661963
JournalBiochemistry
Year2003
Volume42
Pages14507-14
AuthorsNagano S, Shimada H, Tarumi A, Hishiki T, Kimata-Ariga Y, Egawa T, Suematsu M, Park SY, Adachi S, Shiro Y, Ishimura Y
TitleInfrared spectroscopic and mutational studies on putidaredoxin-induced conformational changes in ferrous CO-P450cam.
Related PDB1iwi,1iwj,1iwk
[53]
PubMed ID15522298
JournalJ Mol Biol
Year2004
Volume344
Pages455-69
AuthorsHays AM, Dunn AR, Chiu R, Gray HB, Stout CD, Goodin DB
TitleConformational states of cytochrome P450cam revealed by trapping of synthetic molecular wires.
Related PDB1re9,1rf9
[54]
PubMed ID15269210
JournalJ Biol Chem
Year2004
Volume279
Pages42844-9
AuthorsNagano S, Tosha T, Ishimori K, Morishima I, Poulos TL
TitleCrystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding.
Related PDB1t85,1t86,1t87,1t88
[55]
PubMed ID15219983
JournalJ Inorg Biochem
Year2004
Volume98
Pages1175-82
AuthorsWade RC, Winn PJ, Schlichting I, Sudarko
TitleA survey of active site access channels in cytochromes P450.
Related PDB1uyu
[56]
PubMed ID15858263
JournalActa Crystallogr D Biol Crystallogr
Year2005
Volume61
Pages539-44
AuthorsMeilleur F, Dauvergne MT, Schlichting I, Myles DA
TitleProduction and X-ray crystallographic analysis of fully deuterated cytochrome P450cam.
Related PDB1yrc,1yrd
[57]
PubMed ID15994329
JournalJ Biol Chem
Year2005
Volume280
Pages31659-63
AuthorsNagano S, Poulos TL
TitleCrystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism.
Related PDB2a1m,2a1n,2a1o
[58]
PubMed ID16510191
JournalJ Inorg Biochem
Year2006
Volume100
Pages507-18
AuthorsMakris TM, von Koenig K, Schlichting I, Sligar SG
TitleThe status of high-valent metal oxo complexes in the P450 cytochromes.
Related PDB2fe6,2fer,2feu
[59]
PubMed ID16943206
JournalProtein Eng Des Sel
Year2006
Volume19
Pages491-6
AuthorsVerras A, Alian A, de Montellano PR
TitleCytochrome P450 active site plasticity: attenuation of imidazole binding in cytochrome P450(cam) by an L244A mutation.
Related PDB2h7q,2h7r,2h7s
[60]
PubMed ID17962225
JournalProtein Eng Des Sel
Year2007
Volume20
Pages473-80
AuthorsXu F, Bell SG, Rao Z, Wong LL
TitleStructure-activity correlations in pentachlorobenzene oxidation by engineered cytochrome P450cam.
Related PDB2frz,2gqz,2gr6
[61]
PubMed ID18001135
JournalBiochemistry
Year2007
Volume46
Pages14129-40
AuthorsMakris TM, von Koenig K, Schlichting I, Sligar SG
TitleAlteration of P450 distal pocket solvent leads to impaired proton delivery and changes in heme geometry.
Related PDB2qbl,2qbm,2qbn,2qbo
[62]
PubMed ID18088124
JournalJ Am Chem Soc
Year2008
Volume130
Pages432-3
AuthorsHarada K, Sakurai K, Ikemura K, Ogura T, Hirota S, Shimada H, Hayashi T
TitleEvaluation of the functional role of the heme-6-propionate side chain in cytochrome P450cam.
Related PDB2zaw,2zax

comments
Putidaredoxin (PDB;1oqq) is a electron-transfer protein from Pseudomonas putida, which is homologous to ferredoxin (PDB;1a70), with [2Fe-2S] as a cofactor. This enzyme accepts one electron at a time from putidaredoxin, indicating that the two association-dissociation interactions between this enzyme and putidaredoxin occur.
(A) Electron transfer from [2Fe-2S] (of putidaredoxin) to heme group of this enzyme, reducing the heme-iron from the ferric (FeIII) to the ferrous state (FeII):
(A1) Indirect transfer from [2Fe-2S] to Asp38 through Cys39 (bound to [2Fe-2S]) (of putidaredoxin).
(A2) Indirect transfer from Asp38 (of putidaredoxin) to Heme propionate group (acidic group) through Arg112 (of this enzyme) (see [31]).
(C) Electron transfer from [2Fe-2S] (of putidaredoxin) to heme group of this enzyme, decomposing the oxygenated intermediate:
The following reactions involve proton shuttle through Lys178, Arg186, Asp251, Thr252 (see [37], [41]).
(B) Oxygenation of camphor by O2 at heme, giving 5-hydroxycamphor and water (H2O):
(B1) Peroxygenation step from O2 to produce O-OH:
(B2) Water(H2O) release from the active site:
(B3) Hydroxylation step of camphor:

createdupdated
2004-10-212009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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