Information on EC 1.14.13.B1 - camphor 1,6-monooxygenase

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The expected taxonomic range for this enzyme is: Pseudomonas putida

EC NUMBER
COMMENTARY hide
1.14.13.B1
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
camphor 1,6-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(-)-bornane-2,5-dione + reduced rubredoxin + O2 + 2 H+ = 1,8,8-trimethyl-2-oxabicyclo[3.2.1]octane-3,6-dione + oxidized rubredoxin + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Bayer-Villiger reaction
oxidation
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-
-
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redox reaction
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-
-
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reduction
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-
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SYSTEMATIC NAME
IUBMB Comments
(-)-camphor,reduced-rubredoxin:oxygen oxidoreductase (1,6-lactonizing)
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CAS REGISTRY NUMBER
COMMENTARY hide
151616-60-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-camphor + NADH + O2
? + NAD+ + H2O
show the reaction diagram
(+/-)-cis-bicyclo[3.2.0]hept-2-en-6-one + NADH + O2
?
show the reaction diagram
(-)-bornane-2,5-dione + NADH + O2
1,8,8-trimethyl-2-oxabicyclo[3.2.1]octane-3,6-dione + NAD+ + H2O
show the reaction diagram
(-)-bornane-2,5-dione + NADH + O2
?
show the reaction diagram
(-)-bornanone + NADH + O2
?
show the reaction diagram
-
i.e. (-)-camphor
-
-
?
(-)-camphor + NADH + O2
? + NAD+ + H2O
show the reaction diagram
(R,R)-bicyclo[2.2.1]heptane-2,5-dione + NADH + O2
?
show the reaction diagram
2,3,4,5-tetramethyl-2-cyclopenten-1-one + NADH + O2
?
show the reaction diagram
2-cyclohexen-1-one + NADH + O2
?
show the reaction diagram
50% conversion
-
-
?
2-cyclopenten-1-one + NADH + O2
?
show the reaction diagram
48% conversion
-
-
?
2-decanone + NADH + O2
?
show the reaction diagram
11% conversion
-
-
?
3,5,5-trimethyl-2-cyclohexen-1-one + NADH + O2
?
show the reaction diagram
21% conversion
-
-
?
3-methyl-2-cyclohexen-1-one + NADH + O2
?
show the reaction diagram
20% conversion
-
-
?
3-methyl-2-cyclopenten-1-one + NADH + O2
?
show the reaction diagram
10% conversion
-
-
?
4-phenyl-2-butanone + NADH + O2
?
show the reaction diagram
48% conversion
-
-
?
acetophenone + NADH + O2
?
show the reaction diagram
80% conversion
-
-
?
cyclobutanone + NADH + O2
?
show the reaction diagram
13% conversion
-
-
?
cyclohexanone + NADH + O2
?
show the reaction diagram
3% conversion
-
-
?
cyclopentanone + NADH + O2
?
show the reaction diagram
24% conversion
-
-
?
norcamphor + NADH + O2
?
show the reaction diagram
77% conversion
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(-)-bornane-2,5-dione + NADH + O2
?
show the reaction diagram
additional information
?
-
-
catalyzes stereoselective electrophilic biooxidation of a wide range of prochiral organic sulfoxides to the corresponding chiral sulfoxides as well as the nucleophilic biooxidation of ketones to lactones with different enantio- and stereoselectivity, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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FAD is ineffective; purified NADH dehydrogenase component from 2,5-diketocamphane-1,2-monooxygenase can be used as electron donor
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.09
crude extract, at pH 7.5 and 25°C
0.244
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substrate (-)-camphor
0.46
purified enzyme, at pH 7.5 and 25°C
300
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purified enzyme component NADH dehydrogenase
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
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NADH dehydrogenase component, SDS-PAGE
38000
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oxygenating component, gel filtration
40000
x * 40000, SDS-PAGE
40300
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oxygenating component, native PAGE
76000
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both components, ultracentrifugal analysis
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
plate shaped crystals from 4.0 M sodium formate and 28% PEG 8000 in 0.2 M sodium acetate, X-ray analysis
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both components
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HisTrap column chromatography
oxygenating component
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis