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Information on EC 1.14.14.108 - 2,5-diketocamphane 1,2-monooxygenase
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1.14.14.108 2,5-diketocamphane 1,2-monooxygenaseIUBMB Comments
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 and adamantanone . The product spontaneously converts to [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate.
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Word Map
- 1.14.14.108
- putida
-
baeyer-villiger
- flavin
-
bicyclic
-
ncimb
- flavoproteins
- ketone
-
bvmos
-
revisit
-
two-component
- lactone
-
biooxidations
-
requisite
-
recombinantly
-
biocatalysts
- mononucleotide
-
fmn-dependent
- fad
-
+-camphor
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
2,5-diketocamphane 1,2-monooxygenase, 2,5-dkcmo, 3,6-diketocamphane 1,6-monooxygenase, 2,5-dkcmo-1, came25-2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,5-diketocamphane 1,2-monooxygenase
2,5-diketocamphane lactonizing enzyme
-
-
-
-
2,5-diketocamphane monooxygenase
2,5-DKCMO
2,5-DKCMO-1
2,5-DKCMO-2
3,6-diketocamphane 1,6-monooxygenase
camE25-1
camE25-2
camphor ketolactonase I
-
-
-
-
EC 1.14.13.162
-
-
formerly
-
EC 1.14.15.2
-
-
formerly
-
ketolactonase I
-
-
-
-
oxygenase, camphor 1,2-mono
-
-
-
-
additional information
-
2 diketocamphane monooxygenases in Pseudomonas putida
2,5-diketocamphane 1,2-monooxygenase
-
higher regio- and enatioselectivity than isoform 3,6-diketocamphane-1,6-monooxygenase
2,5-diketocamphane 1,2-monooxygenase
-
higher regio- and enatioselectivity than isoform 3,6-diketocamphane-1,6-monooxygenase
-
3,6-diketocamphane 1,6-monooxygenase
-
different enzyme with similar biochemical properties, immunological cross-reactivity
3,6-diketocamphane 1,6-monooxygenase
-
isoenzyme, enantiocomplementary and isofunctional isozymes 2,5-DKCMO EC 1.14.15.2 and 3,6-DKCMO EC 1.14.15.x
3,6-diketocamphane 1,6-monooxygenase
-
isoform, which is probably a different enzyme, i.e. 3,6-DKCMO
3,6-diketocamphane 1,6-monooxygenase
Pseudomonas putida C1 / ATCC 17453
-
different enzyme with similar biochemical properties, immunological cross-reactivity
-
3,6-diketocamphane 1,6-monooxygenase
-
isoenzyme, enantiocomplementary and isofunctional isozymes 2,5-DKCMO EC 1.14.15.2 and 3,6-DKCMO EC 1.14.15.x
-
3,6-diketocamphane 1,6-monooxygenase
-
isoform, which is probably a different enzyme, i.e. 3,6-DKCMO
-
camE25-1
gene name, two isofunctional 2,5-DKCMO genes (camE25-1 for 2,5-DKCMO-1 and camE25-2 for 2,5-DKCMO-2)
camE25-1
gene name, two isofunctional 2,5-DKCMO genes (camE25-1 for 2,5-DKCMO-1 and camE25-2 for 2,5-DKCMO-2)
-
camE25-2
gene name, two isofunctional 2,5-DKCMO genes (camE25-1 for 2,5-DKCMO-1 and camE25-2 for 2,5-DKCMO-2)
camE25-2
gene name, two isofunctional 2,5-DKCMO genes (camE25-1 for 2,5-DKCMO-1 and camE25-2 for 2,5-DKCMO-2)
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
mechanism
-
(+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
catalysis of 2 mechanistically different types of biochemical reactions within the confines of the same active site
-
(+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
higher activity in lactonization of ketones than in oxidation of sulfides to the corresponding sulfoxides
-
(+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
belongs to group of Bayer-Villiger monooxygenases of the NADH plus FMN-dependent type 2 enzymes
-
(+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
cubic space active site model, topography
-
(+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
mechanism
Pseudomonas putida C1 / ATCC 17453
-
-
(+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
mechanism
-
-
(+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
catalysis of 2 mechanistically different types of biochemical reactions within the confines of the same active site
-
-
(+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
higher activity in lactonization of ketones than in oxidation of sulfides to the corresponding sulfoxides
-
-
(+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
belongs to group of Bayer-Villiger monooxygenases of the NADH plus FMN-dependent type 2 enzymes
-
-
(+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
cubic space active site model, topography
-
-
(+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Baeyer-Villiger reaction
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(+)-bornane-2,5-dione,FMNH2:oxygen oxidoreductase (1,2-lactonizing)
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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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
(+)-5-oxo-1,2-campholide + FAD + H2O
(+)-bornane-2,5-dione + FADH2 + O2
-
-
-
-
r
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + 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 + FMNH2 + O2
(+)-5-oxo-1,2-campholide + FMN + H2O
the enzyme is involved in the degradation of (-)-camphor
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
(+)-5-oxo-1,2-campholide + FMN + H2O
the enzyme requires a dedicated NADH-FMN reductase (FMN reductase (NADH)), FMN-dependent two-component monooxygenase system
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
(+)-5-oxo-1,2-campholide + FMN + H2O
the enzyme is involved in the degradation of (-)-camphor
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
(+)-5-oxo-1,2-campholide + FMN + H2O
the enzyme requires a dedicated NADH-FMN reductase (FMN reductase (NADH)), FMN-dependent two-component monooxygenase system
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O
-
flavin reduction during reaction is reversible
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O
-
i.e. 2,5-diketocamphane
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O
-
i.e. 2,5-diketocamphane
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + 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 + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O
Pseudomonas putida C1 / ATCC 17453
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O
Pseudomonas putida C1 / ATCC 17453
-
i.e. 2,5-diketocamphane
i.e. cyclopentenoic acid
?
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O
Pseudomonas putida C1 / ATCC 17453
-
i.e. 2,5-diketocamphane
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O
-
i.e. 2,5-diketocamphane
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + 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 + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O
-
i.e. 2,5-diketocamphane
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
?
-
inducible by growth on (+)-camphor
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
?
-
i.e. 2,5-diketocamphane, reaction in camphor catabolism of Pseudomonas putida
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
?
-
inducible by growth on racemic camphor
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
?
-
inducible by growth on racemic camphor
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
?
-
inducible by growth on (+)-camphor
-
-
?
(+)-bornanone + FMNH2 + O2
1,2-campholide + FMN + H2O
-
(+)-camphor
-
?
(+)-bornanone + FMNH2 + O2
1,2-campholide + FMN + H2O
-
(+)-camphor
-
?
(+)-bornanone + FMNH2 + O2
1,2-campholide + FMN + H2O
-
(+)-camphor
-
?
(+)-bornanone + FMNH2 + O2
1,2-campholide + FMN + H2O
-
(+)-camphor
-
?
(+)-bornanone + FMNH2 + O2
1,2-campholide + FMN + H2O
-
(+)-camphor
-
?
(+)-bornanone + FMNH2 + O2
1,2-campholide + FMN + H2O
Pseudomonas putida C1 / ATCC 17453
-
(+)-camphor
-
?
(+)-bornanone + FMNH2 + O2
1,2-campholide + FMN + H2O
Pseudomonas putida C1 / ATCC 17453
-
(+)-camphor
-
?
(+)-bornanone + FMNH2 + O2
1,2-campholide + FMN + H2O
Pseudomonas putida C1 / ATCC 17453
-
(+)-camphor
-
?
(+)-bornanone + FMNH2 + O2
1,2-campholide + FMN + H2O
-
(+)-camphor
-
?
(+)-bornanone + FMNH2 + O2
1,2-campholide + FMN + H2O
-
-
-
?
(+)-camphor + FMNH2 + O2
?
conversion to lactone, no concersion of (-)-camphor
-
-
?
(+)-camphor + FMNH2 + O2
?
conversion to lactone, no concersion of (-)-camphor
-
-
?
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 + FMNH2 + O2
3-(1-hydroxy-1-methylethyl)-6-oxoheptanoic acid + FMN + H2O
-
-
-
?
6-oxocineole + FMNH2 + O2
3-(1-hydroxy-1-methylethyl)-6-oxoheptanoic acid + FMN + H2O
Pseudomonas putida C1 / ATCC 17453
-
-
-
?
7,7-dimethylbicyclo[3.2.0] hept-2-en-6-one + FMNH2 + O2
?
-
products: (1S,5R)-3-oxa-lactone (more than 95% enantiomeric excess) and (1R,5S)-2-oxa (more than 80% enantiomeric excess)
-
-
?
7,7-dimethylbicyclo[3.2.0] hept-2-en-6-one + FMNH2 + O2
?
-
products: (1S,5R)-3-oxa-lactone (more than 95% enantiomeric excess) and (1R,5S)-2-oxa (more than 80% enantiomeric excess)
-
-
?
7endo-methylbicyclo[3.2.0]hept-2-en-6-one + FMNH2 + O2
?
-
products: (1S,5R)-3-oxalactone (more than 95% enantiomeric excess) and (1R,5S)-2-oxa (80% enantiomeric excess)
-
-
?
7endo-methylbicyclo[3.2.0]hept-2-en-6-one + FMNH2 + O2
?
-
products: (1S,5R)-3-oxalactone (more than 95% enantiomeric excess) and (1R,5S)-2-oxa (80% enantiomeric excess)
-
-
?
bicyclo[3.2.0]hept-2-en-6-one + FMNH2 + O2
?
-
products: (1S,5R)-3-oxa-lactone (more than 95% enantiomeric excess) and (1R,5S)-2-oxa-lactone (89% enantiomeric excess)
-
-
?
bicyclo[3.2.0]hept-2-en-6-one + FMNH2 + O2
?
-
products: (1S,5R)-3-oxa-lactone (more than 95% enantiomeric excess) and (1R,5S)-2-oxa-lactone (89% enantiomeric excess)
-
-
?
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 SUBSTRATE
NATURAL 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 + FMNH2 + O2
(+)-5-oxo-1,2-campholide + FMN + H2O
the enzyme is involved in the degradation of (-)-camphor
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
(+)-5-oxo-1,2-campholide + FMN + H2O
the enzyme is involved in the degradation of (-)-camphor
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
?
-
inducible by growth on (+)-camphor
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
?
-
i.e. 2,5-diketocamphane, reaction in camphor catabolism of Pseudomonas putida
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
?
-
inducible by growth on racemic camphor
-
-
?
(+)-bornane-2,5-dione + FMNH2 + O2
?
-
inducible by growth on racemic camphor
-
-
?
(+)-bornane-2,5-dione + FMNH2 + 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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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INHIBITOR
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
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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
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substrate (+)-camphor, purified, reconstituted multimeric enzyme complex
additional information
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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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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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brenda