KEGG   ENZYME: 1.14.15.1Help
Entry
EC 1.14.15.1                Enzyme                                 

Name
camphor 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
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
(+)-camphor,reduced putidaredoxin:oxygen oxidoreductase (5-hydroxylating)
Reaction(IUBMB)
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O [RN:R03818]
Reaction(KEGG)
Substrate
(+)-camphor [CPD:C00808];
reduced putidaredoxin;
O2 [CPD:C00007]
Product
(+)-exo-5-hydroxycamphor [CPD:C03448];
oxidized putidaredoxin [CPD:C03302];
H2O [CPD:C00001]
Comment
A heme-thiolate protein (P-450). Also acts on (-)-camphor and 1,2-campholide, forming 5-exo-hydroxy-1,2-campholide.
History
EC 1.14.15.1 created 1972, modified 1986
Reference
1  [PMID:4378858]
  Authors
Hedegaard J, Gunsalus IC.
  Title
Mixed function oxidation. IV. An induced methylene hydroxylase in camphor oxidation.
  Journal
J. Biol. Chem. 240 (1965) 4038-43.
Reference
2  [PMID:4341491]
  Authors
Tyson CA, Lipscomb JD, Gunsalus IC.
  Title
The role of putidaredoxin and P450 cam  in methylene hydroxylation.
  Journal
J. Biol. Chem. 247 (1972) 5777-84.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
9030-82-4

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