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Enzyme Nomenclature
Information on EC 1.14.13.162 - 2,5-diketocamphane 1,2-monooxygenase
for references in articles please use BRENDA:EC1.14.13.162
Word Map on EC 1.14.13.162
- 1.14.13.162
- putida
- fmn
-
baeyer-villiger
-
bicyclic
- flavin
-
ncimb
- ketone
-
recombinantly
-
revisited
- mononucleotide
-
bvmos
-
+-camphor
- synthesis
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The expected taxonomic range for this enzyme is: Pseudomonas putida
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EC NUMBER 
COMMENTARY 
1.14.13.162
-
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RECOMMENDED NAME
GeneOntology No.
2,5-diketocamphane 1,2-monooxygenase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(+)-bornane-2,5-dione + O2 + NADH + H+ = (+)-5-oxo-1,2-campholide + NAD+ + H2O
mechanism
-
(+)-bornane-2,5-dione + O2 + NADH + H+ = (+)-5-oxo-1,2-campholide + NAD+ + 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 lactonization of ketones than in oxidation of sulfides to the corresponding sulfoxides; mechanism
-
(+)-bornane-2,5-dione + O2 + NADH + H+ = (+)-5-oxo-1,2-campholide + NAD+ + H2O
belongs to group of Bayer-Villiger monooxygenases of the NADH plus FMN-dependent type 2 enzymes; mechanism
-
(+)-bornane-2,5-dione + O2 + NADH + H+ = (+)-5-oxo-1,2-campholide + NAD+ + H2O
mechanism
Pseudomonas putida C1 / ATCC 17453
-
-
(+)-bornane-2,5-dione + O2 + NADH + H+ = (+)-5-oxo-1,2-campholide + NAD+ + H2O
belongs to group of Bayer-Villiger monooxygenases of the NADH plus FMN-dependent type 2 enzymes; 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 lactonization of ketones than in oxidation of sulfides to the corresponding sulfoxides; mechanism; mechanism
-
-
(+)-bornane-2,5-dione + O2 + NADH + H+ = (+)-5-oxo-1,2-campholide + NAD+ + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Bayer-Villiger reaction
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
(+)-bornane-2,5-dione,NADH:oxygen oxidoreductase (1,2-lactonizing)
A flavoprotein (FMN) which requires Fe2+. A Baeyer-Villiger monooxygenase isolated from camphor-grown strains of Pseudomonas putida and encoded on the cam plasmid. Involved in the degradation of (+)-camphor. Requires a dedicated NADH-FMN reductase [cf. EC 1.5.1.42, FMN reductase (NADH)] [1-3]. Can accept several bicyclic ketones including (+)- and (-)-camphor [6] and adamantanone [4].
The product spontaneously converts to [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate.
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CAS REGISTRY NUMBER
COMMENTARY
37256-81-8
-
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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
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
1,3,3-trimethyl-2-oxabicyclo-(2,2,2)octane + NADH + O2
1,6,6-trimethyl-2,7-dioxa(3,2,2)bicyclononan-3-one + NAD+ + H2O
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
-
flavin reduction during reaction is reversible
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
-
i.e. 2,5-diketocamphane
-
?
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
-
i.e. 2,5-diketocamphane
-
-
?
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
-
i.e. 2,5-diketocamphane
product is an unstable lactone-intermediate and forms spontaneously 2-oxo-DELTA3-4,5,5-trimethylcyclopentenyl acetic acid
?
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
Pseudomonas putida C1 / ATCC 17453
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
Pseudomonas putida C1 / ATCC 17453
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
Pseudomonas putida C1 / ATCC 17453
-
i.e. 2,5-diketocamphane
-
-
?
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
-
i.e. 2,5-diketocamphane
-
?
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
-
i.e. 2,5-diketocamphane
product is an unstable lactone-intermediate and forms spontaneously 2-oxo-DELTA3-4,5,5-trimethylcyclopentenyl acetic acid
?
(+)-bornane-2,5-dione + NADH + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + NAD+ + H2O
-
i.e. 2,5-diketocamphane
-
-
?
(+)-bornane-2,5-dione + NADH + O2
?
-
inducible by growth on (+)-camphor
-
-
?
(+)-bornane-2,5-dione + NADH + O2
?
-
i.e. 2,5-diketocamphane, reaction in camphor catabolism of Pseudomonas putida
-
-
?
(+)-bornane-2,5-dione + NADH + O2
?
-
inducible by growth on racemic camphor
-
-
?
(+)-bornane-2,5-dione + NADH + O2
?
-
inducible by growth on racemic camphor
-
-
?
(+)-bornane-2,5-dione + NADH + O2
?
-
inducible by growth on (+)-camphor
-
-
?
(+)-bornanone + NADH + O2
1,2-campholide + NAD+ + H2O
-
(+)-camphor
-
?
(+)-bornanone + NADH + O2
1,2-campholide + NAD+ + H2O
-
(+)-camphor
-
?
(+)-bornanone + NADH + O2
1,2-campholide + NAD+ + H2O
-
(+)-camphor
-
?
(+)-bornanone + NADH + O2
1,2-campholide + NAD+ + H2O
-
(+)-camphor
-
?
(+)-bornanone + NADH + O2
1,2-campholide + NAD+ + H2O
-
(+)-camphor
-
?
(+)-bornanone + NADH + O2
1,2-campholide + NAD+ + H2O
Pseudomonas putida C1 / ATCC 17453
-
(+)-camphor
-
?
(+)-bornanone + NADH + O2
1,2-campholide + NAD+ + H2O
Pseudomonas putida C1 / ATCC 17453
-
(+)-camphor
-
?
(+)-bornanone + NADH + O2
1,2-campholide + NAD+ + H2O
Pseudomonas putida C1 / ATCC 17453
-
(+)-camphor
-
?
(+)-bornanone + NADH + O2
1,2-campholide + NAD+ + H2O
-
-
-
?
1,3,3-trimethyl-2-oxabicyclo-(2,2,2)octane + NADH + O2
1,6,6-trimethyl-2,7-dioxa(3,2,2)bicyclononan-3-one + NAD+ + H2O
-
6-oxocineole
-
?
1,3,3-trimethyl-2-oxabicyclo-(2,2,2)octane + NADH + O2
1,6,6-trimethyl-2,7-dioxa(3,2,2)bicyclononan-3-one + NAD+ + H2O
Pseudomonas putida C1 / ATCC 17453
-
6-oxocineole
-
?
6-oxocineole + NADH + O2
3-(1-hydroxy-1-methylethyl)-6-oxoheptanoic acid + NAD+ + H2O
-
-
-
?
6-oxocineole + NADH + O2
3-(1-hydroxy-1-methylethyl)-6-oxoheptanoic acid + NAD+ + H2O
Pseudomonas putida C1 / ATCC 17453
-
-
-
?
additional information
?
-
-
enzyme is associated with a NADH oxidase
-
-
-
additional information
?
-
-
enzyme is associated with a NADH oxidase
-
-
-
additional information
?
-
-
several sulfides and bicyclo[3,2,0]hept-2-en-6-one are enantioselectively oxidized to the corresponding sulfoxides and oxa lactones, respectively
-
-
-
additional information
?
-
-
several sulfides and bicyclo[3,2,0]hept-2-en-6-one are enantioselectively oxidized to the corresponding sulfoxides and oxa lactones, respectively
-
-
-
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
-
-
-
additional information
?
-
-
no activity with (-)-camphor and other ketocamphanes that do not possess a keto group at position 2
-
-
-
additional information
?
-
Pseudomonas putida C1 / ATCC 17453
-
enzyme is associated with a NADH oxidase
-
-
-
additional information
?
-
Pseudomonas putida C1 / ATCC 17453
-
no activity with (-)-camphor and other ketocamphanes that do not possess a keto group at position 2
-
-
-
additional information
?
-
-
enzyme is associated with a NADH oxidase
-
-
-
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
-
-
-
additional information
?
-
-
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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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
(+)-bornane-2,5-dione + NADH + O2
?
-
inducible by growth on (+)-camphor
-
-
?
(+)-bornane-2,5-dione + NADH + O2
?
-
i.e. 2,5-diketocamphane, reaction in camphor catabolism of Pseudomonas putida
-
-
?
(+)-bornane-2,5-dione + NADH + O2
?
-
inducible by growth on racemic camphor
-
-
?
(+)-bornane-2,5-dione + NADH + O2
?
-
inducible by growth on racemic camphor
-
-
?
(+)-bornane-2,5-dione + NADH + O2
?
-
inducible by growth on (+)-camphor
-
-
?
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
-
-
-
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
LITERATURE
IMAGE
FAD
-
2 mol will bind reversibly at the binding site of the apoprotein of the dehydrogenase, in the presence of FMN only 1 mol
FMN
-
both enzymatic steps require FMN, not replaceable by GSH, Cys, sodium borohydride or ascorbate
FMN
-
0.4 mol per mol of component E1, 0.7 mol per mol of component E2; components E1 and E2 bind FMN reversibly
NADH
-
interaction of inducible NADH dehydrogenase component via bound FMN with oxygenating component; requirement
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-bipyridine
-
inhibition of the whole enzyme complex, but not of the components alone; reactivation by Fe2+, not by Co2+, Cu2+, Mn2+, Mg2+, Zn2+, Fe3+
2,2'-bipyridine
-
inhibition of the whole enzyme complex, but not of the components alone
p-hydroxymercuribenzoate
-
incomplete inhibition, dehydrogenase, reversible by GSH or DTT
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
boiled cell-free extract, activation, replaces FMN in the assay
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.43
-
substrate (+)-camphor, purified, reconstituted multimeric enzyme complex
additional information
-
no enzyme assay possible in crude extract due to competition with other enzymes for NADH
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
NADH dehydrogenase component forming a loose complex with the oxygenating component
Pseudomonas putida C1 / ATCC 17453
-
; NADH dehydrogenase component forming a loose complex with the oxygenating component
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
120000
additional information
36000
-
reductase component E2, low speed sedimentation without reaching equilibrium
additional information
-
2 electrophoretic components, PAGE at pH 8.9 and higher
additional information
-
multi-component enzyme, consisting of at least two components: a reductase E2 and an oxygenating component E1
additional information
-
multi-component enzyme, consists of FMN-reductase and oxygenase compound
additional information
-
enzyme components form a very loose complex; enzyme consists of 2 components: 1 oxygenating and 1 NADH dehydrogenase
additional information
-
enzyme consists of 2 components: 1 oxygenating and 1 NADH dehydrogenase
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
-
2 electrophoretic components, PAGE at pH 8.9 and higher
additional information
-
multi-component enzyme, consisting of at least two components: a reductase E2 and an oxygenating component E1
additional information
-
enzyme components form a very loose complex; enzyme consists of 2 components: 1 oxygenating and 1 NADH dehydrogenase
additional information
-
enzyme consists of 2 components: 1 oxygenating and 1 NADH dehydrogenase
additional information
Pseudomonas putida C1 / ATCC 17453
-
2 electrophoretic components, PAGE at pH 8.9 and higher; enzyme components form a very loose complex; enzyme consists of 2 components: 1 oxygenating and 1 NADH dehydrogenase
-
additional information
-
enzyme consists of 2 components: 1 oxygenating and 1 NADH dehydrogenase
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal clusters, grown in 0.2 M CaCl2, 0.1 M HEPES and 30% PEG 400, X-ray analysis
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
10 min, component E2 retains full activity, component E3 loses 50%, component E3 loses 90% in the presence of substrate or component E1
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, in 0.05 M Tris/HCl or potassium phosphate buffer, pH 7.2, the dehydrogenase is stable for months
-
-20°C, ammonium sulfate precipitates as frozen pastes stable over a long period of time
-
0°C, in buffer, the dehydrogenase is stable for a week, in very dilute solutions, the dehydrogenase is stable without protective agents
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
inactive enzyme after dialysis can be reactivated by Fe2+ at 0.1 mM, Fe3+, Co2+, Zn2+, Mn2+, Mg2+, and Cu2+ are not usefull for reactivation
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
production of useful chiral synthons for chemoenzymatic synthesis
synthesis
-
production of useful chiral synthons for chemoenzymatic synthesis
-
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.162)
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