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2,5-diketocamphane 1,2-monooxygenase
2,5-diketocamphane lactonizing enzyme
-
-
-
-
2,5-diketocamphane monooxygenase
3,6-diketocamphane 1,6-monooxygenase
camphor ketolactonase I
-
-
-
-
EC 1.14.13.162
-
-
formerly
-
EC 1.14.15.2
-
-
formerly
-
oxygenase, camphor 1,2-mono
-
-
-
-
additional information
-
2 diketocamphane monooxygenases in Pseudomonas putida
2,5-diketocamphane 1,2-monooxygenase
-
-
2,5-diketocamphane 1,2-monooxygenase
-
higher regio- and enatioselectivity than isoform 3,6-diketocamphane-1,6-monooxygenase
2,5-diketocamphane 1,2-monooxygenase
-
-
-
2,5-diketocamphane 1,2-monooxygenase
-
-
-
2,5-diketocamphane 1,2-monooxygenase
-
-
-
2,5-diketocamphane 1,2-monooxygenase
-
higher regio- and enatioselectivity than isoform 3,6-diketocamphane-1,6-monooxygenase
-
2,5-diketocamphane monooxygenase
-
2,5-diketocamphane monooxygenase
-
-
2,5-DKCMO
-
-
2,5-DKCMO-1
-
2,5-DKCMO-2
-
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
-
different enzyme with similar biochemical properties, immunological cross-reactivity
-
3,6-diketocamphane 1,6-monooxygenase
-
-
-
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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(+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
(+)-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
-
-
(+)-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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(+)-5-oxo-1,2-campholide + FAD + H2O
(+)-bornane-2,5-dione + FADH2 + O2
-
-
-
-
r
(+)-bornane-2,5-dione + FMNH2 + O2
(+)-5-oxo-1,2-campholide + FMN + H2O
(+)-bornane-2,5-dione + FMNH2 + O2
3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O
(+)-bornane-2,5-dione + FMNH2 + O2
?
(+)-bornanone + FMNH2 + O2
1,2-campholide + FMN + H2O
(+)-camphor + FMNH2 + O2
?
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 + FMNH2 + O2
3-(1-hydroxy-1-methylethyl)-6-oxoheptanoic acid + FMN + H2O
7,7-dimethylbicyclo[3.2.0] hept-2-en-6-one + FMNH2 + O2
?
7endo-methylbicyclo[3.2.0]hept-2-en-6-one + FMNH2 + O2
?
bicyclo[3.2.0]hept-2-en-6-one + FMNH2 + O2
?
additional information
?
-
(+)-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
-
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
-
-
?
(+)-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
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-
?
(+)-bornane-2,5-dione + FMNH2 + O2
?
-
i.e. 2,5-diketocamphane, reaction in camphor catabolism of Pseudomonas putida
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-
?
(+)-bornane-2,5-dione + FMNH2 + O2
?
-
inducible by growth on racemic camphor
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-
?
(+)-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
-
-
-
?
(+)-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
-
(+)-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 + 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
-
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
-
-
-
?
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
?
-
-
rubredoxin not mentioned
-
-
?
additional information
?
-
-
rubredoxin not mentioned
-
-
?
additional information
?
-
-
rubredoxin not mentioned
-
-
?
additional information
?
-
-
rubredoxin not mentioned
-
-
?
additional information
?
-
-
rubredoxin not mentioned
-
-
?
additional information
?
-
-
rubredoxin not mentioned
-
-
?
additional information
?
-
-
rubredoxin not mentioned
-
-
?
additional information
?
-
-
rubredoxin not mentioned
-
-
?
additional information
?
-
-
rubredoxin not mentioned
-
-
?
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
?
-
-
rubredoxin not mentioned
-
-
?
additional information
?
-
-
rubredoxin not mentioned
-
-
?
additional information
?
-
-
enzyme is associated with a NADH oxidase
-
-
?
additional information
?
-
-
rubredoxin not mentioned
-
-
?
additional information
?
-
-
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
?
-
-
rubredoxin not mentioned
-
-
?
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
?
-
-
rubredoxin not mentioned
-
-
?
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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Williams, D.R.; Trudgill, P.W.; Taylor, D.G.
Metabolism of 1,8-cineole by a Rhodococcus species: Ring cleavage reactions
J. Gen. Microbiol.
135
1957-1967
1989
Pseudomonas putida, Pseudomonas putida C1 / ATCC 17453
-
brenda
Conrad, H.E.; DuBus, R.; Gunsalus, I.C.
An enzyme system for cyclic ketone lactonization
Biochem. Biophys. Res. Commun.
6
293-297
1961
Pseudomonas putida
brenda
Yu, C.A.; Gunsalus, I.C.
Monoxygenases. VII. Camphor ketolactonase I and the role of three protein components
J. Biol. Chem.
244
6149-6152
1969
Pseudomonas putida
brenda
Taylor, D.G.; Trudgill, P.W.
Camphor revisited: studies of 2,5-diketocamphane 1,2-monooxygenase from Pseudomonas putida ATCC 17453
J. Bacteriol.
165
489-497
1986
Pseudomonas putida, Pseudomonas putida C1 / ATCC 17453
brenda
Trudgill, P.W.; DuBus, R.; Gunsalus, I.C.
Mixed function oxidation. V. Flavin interaction with a reduced diphosphopyridine nucleotide dehydrogenase, one of the enzymes participating in camphor lactonization
J. Biol. Chem.
241
1194-1205
1966
Pseudomonas putida
brenda
Trudgill, P.W.; DuBus, R.; Gunsalus, I.C.
Mixed function oxidation. VI. Purification of a tightly coupled electron transport complex in camphor lactonization
J. Biol. Chem.
241
4288-4290
1966
Pseudomonas putida
brenda
Beecher, J.; Willetts, A.
Biotransformation of organic sulfides. Predictive active site models for sulfoxidation catalyzed by 2,5-diketocamphane 1,2-monooxygenase and 3,6-diketocamphane 1,6-monooxygenase, enantiocomplementary enzymes from Pseudomonas putida NCIMB 10007
Tetrahedron
9
1899-1916
1998
Pseudomonas putida, Pseudomonas putida NCIMB 10007
-
brenda
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Pseudomonas putida, Pseudomonas putida C1 / ATCC 17453
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Pseudomonas putida, Pseudomonas putida NCIMB 10007
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Pseudomonas putida, Pseudomonas putida NCIMB 10007
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Camphor pathway redux functional recombinant expression of 2,5- and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions
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Pseudomonas putida (M5AWY0), Pseudomonas putida (Q6STM1), Pseudomonas putida, Pseudomonas putida ATCC 17453 (M5AWY0), Pseudomonas putida ATCC 17453 (Q6STM1), Pseudomonas putida ATCC 17453
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McGhie, E.; Littlechild, J.
The purification and crystallisation of 2,5-diketocamphane 1,2 monooxygenase and 3,6-diketocamphane 1,6 monooxygenase from Pseudomonas putida NCIMB 10007
Biochem. Soc. Trans.
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29S
1996
Pseudomonas putida, Pseudomonas putida ATCC 17453
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Enantioselective oxidations by the diketocamphane monooxygenase isozymes from Pseudomonas putida
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571-576
1996
Pseudomonas putida, Pseudomonas putida ATCC 17453
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Beecher, J.; Willetts, A.
Biotransformation of organic sulfides. Predictive active site models for sulfoxidation catalysed by 2,5-diketocamphane 1,2-monooxygenase and 3,6-diketocamphane 1,6-monooxygenase, enantiocomplementary enzymes from Pseudomonas putida NCIMB 10007
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1998
Pseudomonas putida, Pseudomonas putida ATCC 17453
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