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bornane-2,6-dione + H2O = [(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate
bornane-2,6-dione + H2O = [(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate
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bornane-2,6-dione + H2O = [(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate
analysis of the molecular determinants of both mechanism and enantiotopic selectivity in reactions catalysed by OCH and reaction mechanism, putative Asp154-His145 dyad, overview
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bornane-2,6-dione + H2O = [(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate
involvement of five residues, His45, His122, His145, Asp154, and Glu244, in catalysis, catalytic His145/Asp154 dyad. The the pendant acetate of the product (2S,4S)-alpha-campholinic acid hydrogen bonded to a His145/Asp154 dyad and the endocyclic carbonyl of the cyclopentane ring hydrogen bonds to Trp40, prochiral selectivity, base-catalyzed mechanism of C-C bond cleavage, overview
bornane-2,6-dione + H2O = [(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate
mechanism of carbon-carbon bond cleavage by 6-oxo camphor hydrolase
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bornane-2,6-dione + H2O = [(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate
analysis of the molecular determinants of both mechanism and enantiotopic selectivity in reactions catalysed by OCH and reaction mechanism, putative Asp154-His145 dyad, overview
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bornane-2,6-dione + H2O = [(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate
involvement of five residues, His45, His122, His145, Asp154, and Glu244, in catalysis, catalytic His145/Asp154 dyad. The the pendant acetate of the product (2S,4S)-alpha-campholinic acid hydrogen bonded to a His145/Asp154 dyad and the endocyclic carbonyl of the cyclopentane ring hydrogen bonds to Trp40, prochiral selectivity, base-catalyzed mechanism of C-C bond cleavage, overview
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1-allylbicyclo-[4.3.0]nonane-2,9-dione + H2O
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1-methylbicyclo-[4.3.0]nonane-2,9-dione + H2O
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1-methylbicyclo[5.3.0]decane-2,10-dione + H2O
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6-oxocamphor + H2O
(2R,4S)-alpha-campholinic acid
6-oxocamphor + H2O
(2S,4S)-alpha-campholinic acid
7,7-dimethylbicyclo[2.2.2]octane-2,6-dione + H2O
[(1S)-3,3-dimethyl-5-oxocyclohexyl]acetic acid
8,8-dimethylbicyclo[2.2.2]octane-2,6-dione + H2O
[(1S)-2,2-dimethyl-5-oxocyclohexyl]acetic acid
bicyclo[2.2.2]octan-2,6-dione + H2O
[(1S)-3-oxocyclohexyl]acetic acid
bicyclo[2.2.2]octane-2,6-dione + H2O
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bornane-2,6-dione + H2O
[(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate
additional information
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1-allylbicyclo-[4.3.0]nonane-2,9-dione + H2O
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i.e. 7a-allylhexahydroindene-1,7-dione
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1-allylbicyclo-[4.3.0]nonane-2,9-dione + H2O
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i.e. 7a-allylhexahydroindene-1,7-dione
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1-methylbicyclo-[4.3.0]nonane-2,9-dione + H2O
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OCH catalyses the resolution of 1-methylbicyclo-[4.3.0]nonane-2,9-dione, i.e. 7a-methylhexahydroindene-1,7-dione
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1-methylbicyclo-[4.3.0]nonane-2,9-dione + H2O
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OCH catalyses the resolution of 1-methylbicyclo-[4.3.0]nonane-2,9-dione, i.e. 7a-methylhexahydroindene-1,7-dione
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1-methylbicyclo[5.3.0]decane-2,10-dione + H2O
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i.e. 8a-methyloctahydroazulene-1,8-dione
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1-methylbicyclo[5.3.0]decane-2,10-dione + H2O
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i.e. 8a-methyloctahydroazulene-1,8-dione
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6-oxocamphor + H2O
(2R,4S)-alpha-campholinic acid
the 6-oxocamphor hydrolase catalyzes the desymmetrization of 6-oxocamphor to yield (2R,4S)-alpha-campholinic acid, putative asymmetric hydrolysis mechanism for 6-oxocamphor hydrolase based on sequence homology and the known mechanism of the crotonase enzymes, overview
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6-oxocamphor + H2O
(2R,4S)-alpha-campholinic acid
the 6-oxocamphor hydrolase catalyzes the desymmetrization of 6-oxocamphor to yield (2R,4S)-alpha-campholinic acid, putative asymmetric hydrolysis mechanism for 6-oxocamphor hydrolase based on sequence homology and the known mechanism of the crotonase enzymes, overview
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6-oxocamphor + H2O
(2S,4S)-alpha-campholinic acid
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6-oxocamphor + H2O
(2S,4S)-alpha-campholinic acid
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7,7-dimethylbicyclo[2.2.2]octane-2,6-dione + H2O
[(1S)-3,3-dimethyl-5-oxocyclohexyl]acetic acid
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7,7-dimethylbicyclo[2.2.2]octane-2,6-dione + H2O
[(1S)-3,3-dimethyl-5-oxocyclohexyl]acetic acid
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8,8-dimethylbicyclo[2.2.2]octane-2,6-dione + H2O
[(1S)-2,2-dimethyl-5-oxocyclohexyl]acetic acid
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8,8-dimethylbicyclo[2.2.2]octane-2,6-dione + H2O
[(1S)-2,2-dimethyl-5-oxocyclohexyl]acetic acid
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bicyclo[2.2.2]octan-2,6-dione + H2O
[(1S)-3-oxocyclohexyl]acetic acid
the enzyme 6-oxocamphor hydrolase catalyses the hydrolytic retro-Claisen condensation of non-enolisable, symmetrical beta-diketones leading to optically pure keto acid [(1S)-3-oxocyclohexyl]acetic acid, it catalyses the hydrolysis of bicyclo[2.2.2]octan-2,6-dione to [(1S)-3-oxocyclohexyl]acetic acid with full conversion and perfect stereoselectivity (ee >99%) within three hours
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bicyclo[2.2.2]octan-2,6-dione + H2O
[(1S)-3-oxocyclohexyl]acetic acid
the enzyme 6-oxocamphor hydrolase catalyses the hydrolytic retro-Claisen condensation of non-enolisable, symmetrical beta-diketones leading to optically pure keto acid [(1S)-3-oxocyclohexyl]acetic acid, it catalyses the hydrolysis of bicyclo[2.2.2]octan-2,6-dione to [(1S)-3-oxocyclohexyl]acetic acid with full conversion and perfect stereoselectivity (ee >99%) within three hours
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bornane-2,6-dione + H2O
[(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate
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bornane-2,6-dione + H2O
[(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate
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additional information
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6-oxo camphor hydrolase catalyzes carbon-carbon bond cleavage in bicyclic beta-diketones via a retro-Claisen reaction
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additional information
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modeling of the substrate, 6-oxo camphor, and a proposed enolate intermediate in the putative active site suggesting possible mechanistic roles for Glu244, Asp154, His122, His45, and His145, overview
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additional information
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the transformation catalysed by OCH in nature is the cleavage, by a retro-Claisen reaction, of the bicyclic diketone 6-oxocamphor to alpha-campholinic acid, a reaction that proceeds with high diastereoselectivity and enantioselectivity in favour of the (2R,4S)-enantiomer of the product
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additional information
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substrate specificity and enantioselectivity, competence of the enzyme for kinetic resolutions of asymmetric, racemic substrates, modeling, overview. Increasing the length of the alkyl chain in the 1-position, or enlarging one ofthe rings, increases the enantioselectivity of the enzyme to 5.7 and 3.1 for the substrates 1-allylbicyclo-[4.3.0]nonane-2,9-dione (7a-allylhexahydroindene-1,7-dione) and 1-methylbicyclo[5.3.0]decane-2,10-dione (8a-methyloctahydroazulene-1,8-dione), respectively. 1-Methylbicyclo[5.4.0]undecane-2,10-dione, i.e. 9a-methyloctahydrobenzocycloheptene-1,9-dione, is not a substrate for OCH
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additional information
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prochiral bicyclic diketones are transformed to a single diastereomer of 3-substituted cyclohexylamine derivatives via three consecutive biocatalytic steps. The two chiral centres are set up by the C-C hydrolase 6-oxocamphor hydrolase in the first step and by an omega-transaminase in the last step. The esterification of the intermediate keto acid is catalysed by a lipase in the second step if possible, method overview. The cis- as well as the trans-diastereomers can be obtained in optically pure forms
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additional information
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the transformation catalysed by OCH in nature is the cleavage, by a retro-Claisen reaction, of the bicyclic diketone 6-oxocamphor to alpha-campholinic acid, a reaction that proceeds with high diastereoselectivity and enantioselectivity in favour of the (2R,4S)-enantiomer of the product
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additional information
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substrate specificity and enantioselectivity, competence of the enzyme for kinetic resolutions of asymmetric, racemic substrates, modeling, overview. Increasing the length of the alkyl chain in the 1-position, or enlarging one ofthe rings, increases the enantioselectivity of the enzyme to 5.7 and 3.1 for the substrates 1-allylbicyclo-[4.3.0]nonane-2,9-dione (7a-allylhexahydroindene-1,7-dione) and 1-methylbicyclo[5.3.0]decane-2,10-dione (8a-methyloctahydroazulene-1,8-dione), respectively. 1-Methylbicyclo[5.4.0]undecane-2,10-dione, i.e. 9a-methyloctahydrobenzocycloheptene-1,9-dione, is not a substrate for OCH
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additional information
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prochiral bicyclic diketones are transformed to a single diastereomer of 3-substituted cyclohexylamine derivatives via three consecutive biocatalytic steps. The two chiral centres are set up by the C-C hydrolase 6-oxocamphor hydrolase in the first step and by an omega-transaminase in the last step. The esterification of the intermediate keto acid is catalysed by a lipase in the second step if possible, method overview. The cis- as well as the trans-diastereomers can be obtained in optically pure forms
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selenomethionine-labeled enzyme, vapor diffusion hanging drop technique, protein solution containing 10 mg/ml protein in 50 mM Tris-HCl, pH 7.0, 1 mM dithiothreitol, 0.020 mM phenylmethylsulfonyl fluoride is mixed in a 1:1 ratio with reservoir solution, that contains for the native enzyme, the reservoir solution consisted of 0.1 M sodium acetate buffer, pH 4.5, 0.2 M ammonium sulfate, and 28% v/v PEG 4000, and for the selenomethionyl enzyme 0.1 M MES, pH 5.5, 0.2 M ammonium sulfate, 37.5% v/v 5,000 Da monomethyl ether, and 0.2% w/v n-octyl-beta-D-glucopyranoside, X-ray diffraction structure determination and analysis at 2.0-2.4 A resolution, selenomethionine multiple wave anomalous dispersion, molecular modeling
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OCH mutant H122A in complex with the minor diastereoisomer of (2S,4S)-alpha-campholinic acid, vapor diffusion hanging drop technique, mxing of protein solution containing 10 mg/ml protein in 50 mM Tris-HCl, pH 7.1, 1 mM dithiothreitol, and 0.02 mM phenylmethylsulfonyl fluoride with reservoir solution containing 0.1 M 2-(N-morpholino)ethanesulfonic acid, pH 5.6, 0.2 M calcium acetate, and 26% v/v PEG monomethyl ether 2000, in a 1:1 ratio, soakong of crystals in reservoir solution containing 6-oxocamphor for 30 min, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement
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D154N
site-directed mutagenesis, the OCH mutant shows a greatly reduced value of kcat/Km derived from a very large increase in Km for the native substrate 6-oxo camphor compared to the wild-type enzyme
E244Q
site-directed mutagenesis, the mutant shows reduced value of kcat/Km compared to the wild-type enzyme
H122A
site-directed mutagenesis, structure analysis and comparison to the wild-type enzyme, the mutant shows a greatly reduced value of kcat, and its Km is five times that of the wild-type enzyme. The H122A mutant forms a hexamer, a dimer of trimers, identical to that of the wild-type enzyme
H145A
site-directed mutagenesis, the OCH mutant shows a greatly reduced value of kcat/Km derived from a very large increase in Km for the native substrate 6-oxo camphor compared to the wild-type enzyme
H45A
site-directed mutagenesis, the mutant shows reduced value of kcat/Km compared to the wild-type enzyme
D154N
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site-directed mutagenesis, the OCH mutant shows a greatly reduced value of kcat/Km derived from a very large increase in Km for the native substrate 6-oxo camphor compared to the wild-type enzyme
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E244Q
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site-directed mutagenesis, the mutant shows reduced value of kcat/Km compared to the wild-type enzyme
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H122A
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site-directed mutagenesis, structure analysis and comparison to the wild-type enzyme, the mutant shows a greatly reduced value of kcat, and its Km is five times that of the wild-type enzyme. The H122A mutant forms a hexamer, a dimer of trimers, identical to that of the wild-type enzyme
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H145A
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site-directed mutagenesis, the OCH mutant shows a greatly reduced value of kcat/Km derived from a very large increase in Km for the native substrate 6-oxo camphor compared to the wild-type enzyme
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H45A
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site-directed mutagenesis, the mutant shows reduced value of kcat/Km compared to the wild-type enzyme
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Hill, C.; Lee, C.; Smith, D.; Verma, C.; Grogan, G.
On the resolution of chiral substrates by a retro-Claisenase enzyme: biotransformations of heteroannular bicyclic beta-diketones by 6-oxocamphor hydrolase
Adv. Synth. Catal.
349
1353-1360
2007
Rhodococcus sp., Rhodococcus sp. NCIMB 9784
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brenda
Grogan, G.; Roberts, G.A.; Bougioukou, D.; Turner, N.J.; Flitsch, S.L.
The desymmetrization of bicyclic beta -diketones by an enzymatic retro-Claisen reaction. A new reaction of the crotonase superfamily
J. Biol. Chem.
276
12565-12572
2001
Rhodococcus sp. (Q93TU6), Rhodococcus sp. NCIMB 9784 (Q93TU6)
brenda
Whittingham, J.; Turkenburg, J.; Verma, C.; Walsh, M.; Grogan, G.
The 2-A crystal structure of 6-oxo camphor hydrolase: new structural diversity in the crotonase superfamily
J. Biol. Chem.
278
1744-1750
2003
Rhodococcus erythropolis
brenda
Leonard, P.; Grogan, G.
Structure of 6-oxo camphor hydrolase H122A mutant bound to its natural product, (2S,4S)-alpha-campholinic acid. Mutant structure suggests an atypical mode of transition state binding for a crotonase homolog
J. Biol. Chem.
279
31312-31317
2004
Rhodococcus sp. (Q93TU6), Rhodococcus sp. NCIMB 9784 (Q93TU6)
brenda
Siirola, E.; Mutti, F.; Grischek, B.; Hoefler, S.; Fabian, W.; Grogan, G.; Kroutil, W.
Asymmetric synthesis of 3-substituted cyclohexylamine derivatives from prochiral diketones via three biocatalytic steps
Adv. Synth. Catal.
355
1703-1708
2013
Rhodococcus sp. (Q93TU6), Rhodococcus sp. NCIMB 9784 (Q93TU6)
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brenda