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Overview for MACiE Entry M0133

Version history

General Information

EC Number: 1.14.15.1 (A member of the Oxidoreductases, Acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2, With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor)

Enzyme Name: camphor 5-monooxygenase

Biological Species: Pseudomonas putida (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • P00183 - Camphor 5-monooxygenase

Representative PDB Code: 1yrc - X-RAY CRYSTAL STRUCTURE OF HYDROGENATED CYTOCHROME P450CAM (Resolution = 1.40 Å).

Catalytic CATH Codes:

Display structure information

Overall Reaction:

Image of putidaredoxin

Image of (+)-camphor

Image of oxygen

Image of proton

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Image of oxidised putidaredoxin

Image of (+)-exo-5-hydroxycamphor

Image of water

putidaredoxin
C02069
(+)-camphor
C00808
CHEBI:15396
oxygen
C00007
CHEBI:15379
2 proton
C00080
CHEBI:24636
oxidised putidaredoxin
C03302
(+)-exo-5-hydroxycamphor
C03448
CHEBI:15398
water
C00001
CHEBI:15377

Overall Comment: The equatorial coordination positions of iron are filled by four Nitrogen atoms from the porphyrin ring of Heme (HEM417).


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Stepwise Description of the Reaction

Step 1Putidaredoxin donates a single electron to the Fe(III) centre of the heme cofactor.
Step 2In a homolytic addition, Fe(II) donates a single electron to the dioxygen substrate.
Step 3Putidaredoxin donates a second electron to the bound peroxo moiety, which initiates a proton transfer relay through Thr252, water, Asp251, Arg186 to bulk solvent.
Step 4Both Heme and Iron donate single electrons to the bound peroxo moiety, which eliminates water and initiates a proton transfer relay through Thr252, water, Asp251, Arg186 to bulk solvent.
Step 5The iron-bound oxy group abstracts a hydrogen from the camphor substrate.
Step 6The camphor radical initiates a homolytic substitution, hydroxylating the intermediate to form 5-hydroxycamphor. The iron centre accepts a single electron and water displaces the product

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Catalytic Residues Involved

Type Number Chain Location of Function
Arg 186 A Side Chain
Asp 251 A Side Chain
Thr 252 A Side Chain
Cys 357 A Side Chain
Leu 358 A Main Chain Amide
Gly 359 A Main Chain Amide

Metal Cofactors for M0133

Type Het group Number Chain
iron HEM 417 A Overview

References

  1. V. Guallar et al. (2004), J. Am. Chem. Soc., 126, 8501-8508. Cytochrome P450CAM enzymatic catalysis cycle: a quantum mechanics/molecular mechanics study.
    Medline: 15238007
  2. I. Schlichting et al. (2000), Science, 287, 1615-1622. The catalytic pathway of cytochrome p450cam at atomic resolution.
    Medline: 10698731
  3. J. Zheng et al. (2006), J. Am. Chem. Soc., 128, 13204-13215. QM/MM study of mechanisms for compound I formation in the catalytic cycle of cytochrome P450cam.
    Medline: 17017800

Homologue information for M0133 (1yrc)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB

GOA logo
monooxygenase activity (molecular function)
iron ion binding (molecular function)
cytoplasm (cellular component)
electron carrier activity (molecular function)
oxidoreductase activity (molecular function)
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen (molecular function)
camphor 5-monooxygenase activity (molecular function)
heme binding (molecular function)
metal ion binding (molecular function)
oxidation-reduction process (biological process)
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