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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
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EC NUMBER 
COMMENTARY 
1.14.13.B1
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
camphor 1,6-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
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
(-)-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
belongs to group of Bayer-Villiger monooxygenases of the NADH plus FMN-dependent type 2 enzymes; catalysis of 2 mechanistically different types of biochemical reactions within the confines of the same active site; cubic space active site model, topography; higher activity in oxidation of sulfides to the corresponding sulfoxides than in lactonization of ketones; isozyme, enantiocomplementary and isofunctional isozymes 2,5-DKCMO EC 1.14.15.2 and 3,6-DKCMO EC 1.14.15.x; mechanism
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(-)-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
belongs to group of Bayer-Villiger monooxygenases of the NADH plus FMN-dependent type 2 enzymes; mechanism
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(-)-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
i.e. cyclopentaneacetic acid, 3-hydroxy-2,2,3-trimethyl-5-oxo, delta-lactone, reacts sponaneously to (2,2-dimethyl-5-oxo-cyclopent-3-en-1-yl)acetic acid
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(-)-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
belongs to group of Bayer-Villiger monooxygenases of the NADH plus FMN-dependent type 2 enzymes; mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Bayer-Villiger reaction
oxidation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
(-)-camphor,reduced-rubredoxin:oxygen oxidoreductase (1,6-lactonizing)
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CAS REGISTRY NUMBER
COMMENTARY
151616-60-3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; 2 isozymes termed 2,5-diketocamphane-1,2-monooxygenase and 3,6-diketocamphane-1,6-monooxygenase
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(-)-bornane-2,5-dione + NADH + O2
1,8,8-trimethyl-2-oxabicyclo[3.2.1]octane-3,6-dione + NAD+ + H2O
3,5,5-trimethyl-2-cyclohexen-1-one + NADH + O2
?
21% conversion
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?
(+)-camphor + NADH + O2
? + NAD+ + H2O
88% conversion
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?
(+/-)-cis-bicyclo[3.2.0]hept-2-en-6-one + NADH + O2
?
99% conversion
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?
(+/-)-cis-bicyclo[3.2.0]hept-2-en-6-one + NADH + O2
?
99% conversion
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?
(-)-bornane-2,5-dione + NADH + O2
1,8,8-trimethyl-2-oxabicyclo[3.2.1]octane-3,6-dione + NAD+ + H2O
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6-dione i.e. 3,6-diketocamphane
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?
(-)-bornane-2,5-dione + NADH + O2
1,8,8-trimethyl-2-oxabicyclo[3.2.1]octane-3,6-dione + NAD+ + H2O
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6-dione i.e. 3,6-diketocamphane
i.e. cyclopentaneacetic acid, 3-hydroxy-2,2,3-trimethyl-5-oxo, delta-lactone, i.e. 3,4,4-trimethyl-6-carboxy-methyl-DELTA3-cyclopentenone, product is an unstable lactone-intermediate and forms spontaneously (2,2-dimethyl-5-oxo-cyclopent-3-en-1-yl)acetic acid, i.e. 2-oxo-DELTA3-4,5,5-trimethylcyclopentenyl acetic acid
?
(-)-bornane-2,5-dione + NADH + O2
1,8,8-trimethyl-2-oxabicyclo[3.2.1]octane-3,6-dione + NAD+ + H2O
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6-dione i.e. 3,6-diketocamphane
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?
(-)-bornane-2,5-dione + NADH + O2
?
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inducible by growth on (+)-camphor
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?
(-)-bornane-2,5-dione + NADH + O2
?
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inducible by growth on racemic camphor
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?
(-)-bornane-2,5-dione + NADH + O2
?
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inducible by growth on (+)-camphor
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?
(-)-camphor + NADH + O2
? + NAD+ + H2O
91% conversion
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?
(R,R)-bicyclo[2.2.1]heptane-2,5-dione + NADH + O2
?
26% conversion
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?
(R,R)-bicyclo[2.2.1]heptane-2,5-dione + NADH + O2
?
26% conversion
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?
2,3,4,5-tetramethyl-2-cyclopenten-1-one + NADH + O2
?
43% conversion
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?
2,3,4,5-tetramethyl-2-cyclopenten-1-one + NADH + O2
?
43% conversion
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?
additional information
?
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enzyme is associated with a NADH oxidase
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additional information
?
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enzyme is associated with a NADH oxidase
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additional information
?
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several sulfides and bicyclo[3,2,0]hept-2-en-6-one are enantioselectively oxidized to the corresponding sulfoxides and oxa lactones, respectively
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additional information
?
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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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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(-)-bornane-2,5-dione + NADH + O2
?
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inducible by growth on (+)-camphor
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?
(-)-bornane-2,5-dione + NADH + O2
?
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inducible by growth on racemic camphor
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?
(-)-bornane-2,5-dione + NADH + O2
?
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inducible by growth on (+)-camphor
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
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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NADH
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absolute specificity; interaction of inducible NADH dehydrogenase component via bound FMN with oxygenating component
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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NADH dehydrogenase component forming a loosely complex with the oxygenating component
Pseudomonas putida C1 / ATCC 17453
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NADH dehydrogenase component forming a loosely complex with the oxygenating component
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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enzyme components form a very loose complex; enzyme consists of 2 components: 1 oxygenating and 1 NADH dehydrogenase
additional information
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enzyme consists of 2 components: 1 oxygenating and 1 NADH dehydrogenase
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
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enzyme components from a very loose complex; enzyme consists of 2 components: 1 oxygenating and 1 NADH dehydrogenase
additional information
Pseudomonas putida C1 / ATCC 17453
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enzyme components from a very loose complex; enzyme consists of 2 components: 1 oxygenating and 1 NADH dehydrogenase
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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production of useful chiral synthons for chemoenzymatic synthesis
synthesis
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production of useful chiral synthons for chemoenzymatic synthesis
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.B1)
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