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cyclohexane-1,2-dione + H2O = 6-oxohexanoate
cyclohexane-1,2-dione + H2O = 6-oxohexanoate
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cyclohexane-1,2-dione + H2O = 6-oxohexanoate
catalytic reaction mechanism, overview
cyclohexane-1,2-dione + H2O = 6-oxohexanoate
catalytic reaction mechanism, overview
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cyclohexane-1,2-dione + H2O = 6-oxohexanoate
reaction starts with the monohydrated ketone of cyclohexane-1,2-dione and the thiamine diphosphate-ylide which undergoes a nucleophilic attack on the carbonyl group of cyclohexane-1,2-dione. The subsequent cleavage of the CC bond yields an alpha-carbanion, which is in equilibrium with its corresponding enamine. In the following step, the carbonic acid protonates the alpha-carbanion yielding 6-hydroxyhexanoate-thiamine diphosphate. Finally, the product 6-oxohexanoate is released
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cyclohexane-1,2-dione + H2O = 6-oxohexanoate
the C-C bond cleavage is assumed to be initiated by the attack of the ThDP ylide on the C=O bond of the monohydrate 6 of 1,2-diketone 4 to form the ThDP adduct, a tetrahedral intermediate which breaks down to a carboxylic acid
cyclohexane-1,2-dione + H2O = 6-oxohexanoate
the thiamine diphosphate-dependent enzyme involves a C-C bond ring cleavage of alicyclic compound, catalytic mechanism analysis by quantum mechanics/molecular mechanics, molecular docking simulations and modeling
cyclohexane-1,2-dione + H2O = 6-oxohexanoate
reaction starts with the monohydrated ketone of cyclohexane-1,2-dione and the thiamine diphosphate-ylide which undergoes a nucleophilic attack on the carbonyl group of cyclohexane-1,2-dione. The subsequent cleavage of the CC bond yields an alpha-carbanion, which is in equilibrium with its corresponding enamine. In the following step, the carbonic acid protonates the alpha-carbanion yielding 6-hydroxyhexanoate-thiamine diphosphate. Finally, the product 6-oxohexanoate is released
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cyclohexane-1,2-dione + H2O = 6-oxohexanoate
catalytic reaction mechanism, overview
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cyclohexane-1,2-dione + H2O = 6-oxohexanoate
the C-C bond cleavage is assumed to be initiated by the attack of the ThDP ylide on the C=O bond of the monohydrate 6 of 1,2-diketone 4 to form the ThDP adduct, a tetrahedral intermediate which breaks down to a carboxylic acid
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cyclohexane-1,2-dione + H2O = 6-oxohexanoate
the thiamine diphosphate-dependent enzyme involves a C-C bond ring cleavage of alicyclic compound, catalytic mechanism analysis by quantum mechanics/molecular mechanics, molecular docking simulations and modeling
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cyclohexane-1,2-dione + H2O
6-oxohexanoate
cyclohexane-1,2-dione + H2O
6-oxohexanoate + ?
additional information
?
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cyclohexane-1,2-dione + H2O
6-oxohexanoate
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-
?
cyclohexane-1,2-dione + H2O
6-oxohexanoate
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?
cyclohexane-1,2-dione + H2O
6-oxohexanoate
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conversion of the monohydrated ketone form of cyclohexane-1,2-dione, rather than the monoenol form
enzyme additionally catalyzes NAD+-dependent oxidation of 6-oxohexanoate to adipate
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?
cyclohexane-1,2-dione + H2O
6-oxohexanoate
CDH-catalyzed C-C bond cleavage
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?
cyclohexane-1,2-dione + H2O
6-oxohexanoate
the thiamine diphosphate-dependent enzyme involves a C-C bond ring cleavage of alicyclic compound, conversion mechanism, overview. The substrate cyclohexane-1,2-dione exists in the form of monohydrated ketone in solution, and one of the two hydroxyl groups may exist in its neutral or deprotonated state. Therefore, there are three substrates for the catalytic reaction, which may correspond to different reaction details and energetics. for the reaction of deprotonated state of monohydrated cyclohexane-1,2-dione, two additional proton transfer processes are necessary
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?
cyclohexane-1,2-dione + H2O
6-oxohexanoate
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-
?
cyclohexane-1,2-dione + H2O
6-oxohexanoate
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conversion of the monohydrated ketone form of cyclohexane-1,2-dione, rather than the monoenol form
enzyme additionally catalyzes NAD+-dependent oxidation of 6-oxohexanoate to adipate
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?
cyclohexane-1,2-dione + H2O
6-oxohexanoate
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?
cyclohexane-1,2-dione + H2O
6-oxohexanoate
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?
cyclohexane-1,2-dione + H2O
6-oxohexanoate
CDH-catalyzed C-C bond cleavage
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?
cyclohexane-1,2-dione + H2O
6-oxohexanoate
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?
cyclohexane-1,2-dione + H2O
6-oxohexanoate
the thiamine diphosphate-dependent enzyme involves a C-C bond ring cleavage of alicyclic compound, conversion mechanism, overview. The substrate cyclohexane-1,2-dione exists in the form of monohydrated ketone in solution, and one of the two hydroxyl groups may exist in its neutral or deprotonated state. Therefore, there are three substrates for the catalytic reaction, which may correspond to different reaction details and energetics. for the reaction of deprotonated state of monohydrated cyclohexane-1,2-dione, two additional proton transfer processes are necessary
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?
cyclohexane-1,2-dione + H2O
6-oxohexanoate + ?
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further conversion to adipate using NAD+ as electron acceptor
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?
cyclohexane-1,2-dione + H2O
6-oxohexanoate + ?
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further convertion to adipate using NAD+ as electron acceptor
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?
cyclohexane-1,2-dione + H2O
6-oxohexanoate + ?
degradation of cyclohexane-1,2-dione to 6-oxohexanoate comprises the cleavage of a COC bond adjacent to a carbonyl group. In the subsequent NAD-dependent reaction, 6-oxohexanoate is oxidized to adipate
further convertion to adipate using NAD+ as electron acceptor
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?
cyclohexane-1,2-dione + H2O
6-oxohexanoate + ?
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further conversion to adipate using NAD+ as electron acceptor
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?
cyclohexane-1,2-dione + H2O
6-oxohexanoate + ?
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further convertion to adipate using NAD+ as electron acceptor
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?
cyclohexane-1,2-dione + H2O
6-oxohexanoate + ?
degradation of cyclohexane-1,2-dione to 6-oxohexanoate comprises the cleavage of a COC bond adjacent to a carbonyl group. In the subsequent NAD-dependent reaction, 6-oxohexanoate is oxidized to adipate
further convertion to adipate using NAD+ as electron acceptor
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?
additional information
?
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no substrate: cyclohexanone, cyclohexane-1,3-dione
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?
additional information
?
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the enzyme catalyzes C-C bond cleavage of cyclohexane-1,2-dione to produce 6-oxohexanoic acid as the primary product, presumably followed by oxidation of the latter to adipic acid
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?
additional information
?
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the enzyme catalyzes the C-C bond cleavage of cyclohexane-1,2-dione to 6-oxohexanoate, and the asymmetric benzoin condensation between benzaldehyde and pyruvate
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?
additional information
?
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determination of the catalytic activity of recombinant enzyme CDH, both cleavage of cyclohexane-1,2-dione and the cross-benzoin reaction of benzaldehyde and pyruvate. The enzyme is able to catalyze nonphysiological asymmetric C-C bond formation, the cross-benzoin reaction of benzaldehyde and pyruvate (after decarboxylation) to result in the R-configured 1-hydroxy-1-phenylpropan-2-one (98% ee) is performed on an analytical scale. The recombinant CDH shows the same C-C bond-cleavage and C-C bond-formation activity as the enzyme purified from its native source, Azoarcus sp. strain 22Lin. Enzyme CDH catalyzes the asymmetric cross-benzoin reaction of aromatic aldehydes and (decarboxylated) pyruvate (up to quantitative conversion, 92-99% ee). The enzyme accepts also hydroxybenzaldehydes and nitrobenzaldehydes. On a semipreparative scale, sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde are transformed into the corresponding 2-hydroxy ketone products in high yields
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?
additional information
?
-
most reactions of ThDP-dependent enzymes are realized by a nucleophilic attack of deprotonated/activated C2 atom on a partially positive carbonyl carbon atom of the substrate. In the active site of CDH, the C2 atom of ThDP is in close proximity to one of the carbonyl carbons of CDO. Besides, several surrounding residues such as Asn484, His31', His28', Gln116' and His76' play a crucial role in substrate binding
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?
additional information
?
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the enzme catalyze asymmetric CC bond formation from pyruvate (as donor) and an aldehyde (as acceptor). Thiamine diphosphate-dependent enzymes catalyze the formation of acetoin (3-hydroxybutan-2-one) through one of three different pathways: homocoupling of pyruvate, homocoupling of acetaldehyde, or cross-coupling of acetaldehyde (as acceptor) and pyruvate (as donor). Thiamine diphosphate-dependent cyclohexane-1,2-dione hydrolase is able to form (S)-acetoin with particularly high enantioselectivity (up to 95%ee) by all three pathways. An unprecedented non-acetolactate pathway for the homocoupling of pyruvate explains the high enantioselectivity in the CDH-catalyzed formation of (S)-acetoin, enzymatic formation of highly enantioenriched acetoin from two molecules of pyruvate occurs without the release of acetaldehyde or acetolactate, mechanism, overview
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?
additional information
?
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the enzyme also catalyzes the C-C bond formation using benzaldehyde and pyruvate to form (R)-phenylacetylcarbinol, methylpyruvate or butane-2,3-dione can also serve as donor substrates. The phenylacetylcarbinol product of every active enzyme variant has (R)-configuration with over 99% ee. In the absence of aldehydes, the enzyme catalyzes the decarboxylation and homocoupling of pyruvate to provide (S)-acetoin (3-hydroxybutan-2-one) with remarkably high enantioselectivity up to 93% ee. The recombinant double variant CDH-H28A/N484A shows the opposite behavior and catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol. Several acyloins of tertiary alcohols are formed with 54-94% enantiomeric excess. The wild-type enzyme shows no activity with 1,2-diketone. Substrate specificities and enantioselectivities of wild-type and mutant enzymes, overview
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-
?
additional information
?
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the enzme catalyze asymmetric CC bond formation from pyruvate (as donor) and an aldehyde (as acceptor). Thiamine diphosphate-dependent enzymes catalyze the formation of acetoin (3-hydroxybutan-2-one) through one of three different pathways: homocoupling of pyruvate, homocoupling of acetaldehyde, or cross-coupling of acetaldehyde (as acceptor) and pyruvate (as donor). Thiamine diphosphate-dependent cyclohexane-1,2-dione hydrolase is able to form (S)-acetoin with particularly high enantioselectivity (up to 95%ee) by all three pathways. An unprecedented non-acetolactate pathway for the homocoupling of pyruvate explains the high enantioselectivity in the CDH-catalyzed formation of (S)-acetoin, enzymatic formation of highly enantioenriched acetoin from two molecules of pyruvate occurs without the release of acetaldehyde or acetolactate, mechanism, overview
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?
additional information
?
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no substrate: cyclohexanone, cyclohexane-1,3-dione
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?
additional information
?
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the enzyme catalyzes the C-C bond cleavage of cyclohexane-1,2-dione to 6-oxohexanoate, and the asymmetric benzoin condensation between benzaldehyde and pyruvate
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-
?
additional information
?
-
the enzyme also catalyzes the C-C bond formation using benzaldehyde and pyruvate to form (R)-phenylacetylcarbinol, methylpyruvate or butane-2,3-dione can also serve as donor substrates. The phenylacetylcarbinol product of every active enzyme variant has (R)-configuration with over 99% ee. In the absence of aldehydes, the enzyme catalyzes the decarboxylation and homocoupling of pyruvate to provide (S)-acetoin (3-hydroxybutan-2-one) with remarkably high enantioselectivity up to 93% ee. The recombinant double variant CDH-H28A/N484A shows the opposite behavior and catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol. Several acyloins of tertiary alcohols are formed with 54-94% enantiomeric excess. The wild-type enzyme shows no activity with 1,2-diketone. Substrate specificities and enantioselectivities of wild-type and mutant enzymes, overview
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?
additional information
?
-
the enzyme catalyzes C-C bond cleavage of cyclohexane-1,2-dione to produce 6-oxohexanoic acid as the primary product, presumably followed by oxidation of the latter to adipic acid
-
-
?
additional information
?
-
determination of the catalytic activity of recombinant enzyme CDH, both cleavage of cyclohexane-1,2-dione and the cross-benzoin reaction of benzaldehyde and pyruvate. The enzyme is able to catalyze nonphysiological asymmetric C-C bond formation, the cross-benzoin reaction of benzaldehyde and pyruvate (after decarboxylation) to result in the R-configured 1-hydroxy-1-phenylpropan-2-one (98% ee) is performed on an analytical scale. The recombinant CDH shows the same C-C bond-cleavage and C-C bond-formation activity as the enzyme purified from its native source, Azoarcus sp. strain 22Lin. Enzyme CDH catalyzes the asymmetric cross-benzoin reaction of aromatic aldehydes and (decarboxylated) pyruvate (up to quantitative conversion, 92-99% ee). The enzyme accepts also hydroxybenzaldehydes and nitrobenzaldehydes. On a semipreparative scale, sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde are transformed into the corresponding 2-hydroxy ketone products in high yields
-
-
?
additional information
?
-
most reactions of ThDP-dependent enzymes are realized by a nucleophilic attack of deprotonated/activated C2 atom on a partially positive carbonyl carbon atom of the substrate. In the active site of CDH, the C2 atom of ThDP is in close proximity to one of the carbonyl carbons of CDO. Besides, several surrounding residues such as Asn484, His31', His28', Gln116' and His76' play a crucial role in substrate binding
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?
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cyclohexane-1,2-dione + H2O
6-oxohexanoate
cyclohexane-1,2-dione + H2O
6-oxohexanoate + ?
additional information
?
-
cyclohexane-1,2-dione + H2O
6-oxohexanoate
-
-
-
-
?
cyclohexane-1,2-dione + H2O
6-oxohexanoate
-
-
-
?
cyclohexane-1,2-dione + H2O
6-oxohexanoate
-
-
-
-
?
cyclohexane-1,2-dione + H2O
6-oxohexanoate
-
-
-
?
cyclohexane-1,2-dione + H2O
6-oxohexanoate + ?
-
further conversion to adipate using NAD+ as electron acceptor
-
?
cyclohexane-1,2-dione + H2O
6-oxohexanoate + ?
degradation of cyclohexane-1,2-dione to 6-oxohexanoate comprises the cleavage of a COC bond adjacent to a carbonyl group. In the subsequent NAD-dependent reaction, 6-oxohexanoate is oxidized to adipate
further convertion to adipate using NAD+ as electron acceptor
-
?
cyclohexane-1,2-dione + H2O
6-oxohexanoate + ?
-
further conversion to adipate using NAD+ as electron acceptor
-
?
cyclohexane-1,2-dione + H2O
6-oxohexanoate + ?
degradation of cyclohexane-1,2-dione to 6-oxohexanoate comprises the cleavage of a COC bond adjacent to a carbonyl group. In the subsequent NAD-dependent reaction, 6-oxohexanoate is oxidized to adipate
further convertion to adipate using NAD+ as electron acceptor
-
?
additional information
?
-
the enzyme catalyzes C-C bond cleavage of cyclohexane-1,2-dione to produce 6-oxohexanoic acid as the primary product, presumably followed by oxidation of the latter to adipic acid
-
-
?
additional information
?
-
the enzyme catalyzes the C-C bond cleavage of cyclohexane-1,2-dione to 6-oxohexanoate, and the asymmetric benzoin condensation between benzaldehyde and pyruvate
-
-
?
additional information
?
-
the enzyme catalyzes the C-C bond cleavage of cyclohexane-1,2-dione to 6-oxohexanoate, and the asymmetric benzoin condensation between benzaldehyde and pyruvate
-
-
?
additional information
?
-
the enzyme catalyzes C-C bond cleavage of cyclohexane-1,2-dione to produce 6-oxohexanoic acid as the primary product, presumably followed by oxidation of the latter to adipic acid
-
-
?
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evolution
the ring-cleaving cyclohexane-1,2-dione hydrolase is a member of the thiamine diphosphate enzyme family
evolution
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the ring-cleaving cyclohexane-1,2-dione hydrolase is a member of the thiamine diphosphate enzyme family
evolution
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the ring-cleaving cyclohexane-1,2-dione hydrolase is a member of the thiamine diphosphate enzyme family
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metabolism
in the biodegradation pathway of cyclohexane-1,2-diol by Azoarcus sp. strain 22Lin, the last two degradation steps, a biodegradation pathway for alpha-diketones, are catalyzed by cyclohexane-1,2-dione hydrolase
metabolism
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in the biodegradation pathway of cyclohexane-1,2-diol by Azoarcus sp. strain 22Lin, the last two degradation steps, a biodegradation pathway for alpha-diketones, are catalyzed by cyclohexane-1,2-dione hydrolase
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physiological function
CDH catalyses a key step of an anaerobic degradation pathway for alicyclic alcohols by converting cyclohexane-1,2-dione to 6-oxohexanoate and further to adipate using NAD+ as electron acceptor
physiological function
-
CDH catalyses a key step of an anaerobic degradation pathway for alicyclic alcohols by converting cyclohexane-1,2-dione to 6-oxohexanoate and further to adipate using NAD+ as electron acceptor
physiological function
thiamine diphosphate-dependent cyclohexane-1,2-dione hydrolase is the key enzyme of an anaerobic degradation pathway of alicyclic alcohols
physiological function
-
CDH catalyses a key step of an anaerobic degradation pathway for alicyclic alcohols by converting cyclohexane-1,2-dione to 6-oxohexanoate and further to adipate using NAD+ as electron acceptor
-
physiological function
-
thiamine diphosphate-dependent cyclohexane-1,2-dione hydrolase is the key enzyme of an anaerobic degradation pathway of alicyclic alcohols
-
additional information
the active site funnel is rearranged in an unprecedented manner providing the structural basis for the specific binding and cleavage of an alicyclic compound, including a decreased and displaced funnel entrance, a semicircularly shaped loop segment preceding the C-terminal arm and the attachment of the C-terminal arm to other subunits of the CDH tetramer, asymmetry of the two active sites, architecture of the active site funnel of CDH in comparison with other ThDP dependent enzymes, overview
additional information
-
the active site funnel is rearranged in an unprecedented manner providing the structural basis for the specific binding and cleavage of an alicyclic compound, including a decreased and displaced funnel entrance, a semicircularly shaped loop segment preceding the C-terminal arm and the attachment of the C-terminal arm to other subunits of the CDH tetramer, asymmetry of the two active sites, architecture of the active site funnel of CDH in comparison with other ThDP dependent enzymes, overview
additional information
enzyme structure and active site structure analysis from the enzyme-substrate complex crystal structure, PDB ID 2PGN
additional information
wild-type and mutant H28A/N484A active site structure analysis, PDB IDs 2PGN and 4D5G
additional information
-
the active site funnel is rearranged in an unprecedented manner providing the structural basis for the specific binding and cleavage of an alicyclic compound, including a decreased and displaced funnel entrance, a semicircularly shaped loop segment preceding the C-terminal arm and the attachment of the C-terminal arm to other subunits of the CDH tetramer, asymmetry of the two active sites, architecture of the active site funnel of CDH in comparison with other ThDP dependent enzymes, overview
-
additional information
-
wild-type and mutant H28A/N484A active site structure analysis, PDB IDs 2PGN and 4D5G
-
additional information
-
enzyme structure and active site structure analysis from the enzyme-substrate complex crystal structure, PDB ID 2PGN
-
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H28A
site-directed mutagenesis, the mutant enzyme is much less able to catalyze the C-C bond formation as the wild-type enzyme, while the ability for C-C bond cleavage is still intact, the H28A variant shows an 8fold decrease in the formation of (R)-phenylacetylcarbinol (12%), but 1,2-diketone cleavage is nearly unaffected (78% conversion)
H28A/N484A
site-directed mutagenesis, the double mutant catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol, variant H28A/N484A shows acceptable formation of (R)-phenylacetylcarbinol (73%), but conversion toward the cleavage product is decreased by a factor of five (17% conversion), the mutant is also active with 1,2-diketone in contrast to the wild-type enzyme, mutant substrate specificity amd enantioselectivity, overview
H76A
site-directed mutagenesis, inactive mutant
H76A/Q116A
site-directed mutagenesis, inactive mutant
Q116A
site-directed mutagenesis, inactive mutant
H28A
-
site-directed mutagenesis, the mutant enzyme is much less able to catalyze the C-C bond formation as the wild-type enzyme, while the ability for C-C bond cleavage is still intact, the H28A variant shows an 8fold decrease in the formation of (R)-phenylacetylcarbinol (12%), but 1,2-diketone cleavage is nearly unaffected (78% conversion)
-
H28A/N484A
-
site-directed mutagenesis, the double mutant catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol, variant H28A/N484A shows acceptable formation of (R)-phenylacetylcarbinol (73%), but conversion toward the cleavage product is decreased by a factor of five (17% conversion), the mutant is also active with 1,2-diketone in contrast to the wild-type enzyme, mutant substrate specificity amd enantioselectivity, overview
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H76A
-
site-directed mutagenesis, inactive mutant
-
Q116A
-
site-directed mutagenesis, inactive mutant
-
additional information
substrate specificities and enantioselectivities of wild-type and mutant enzymes, overview
additional information
-
substrate specificities and enantioselectivities of wild-type and mutant enzymes, overview
-
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Harder, J.
Anaerobic degradation of cyclohexane-1,2-diol by a new Azoarcus species
Arch. Microbiol.
168
199-204
1997
Azoarcus sp., Azoarcus sp. 22Lin
-
brenda
Fraas, S.; Steinbach, A.; Tabbert, A.; Harder, J.; Ermler, U.; Tittmann, K.; Meyer, A.; Kroneck, P.
Cyclohexane-1,2-dione hydrolase: A new tool to degrade alicyclic compounds
J. Mol. Catal. B
61
47-49
2009
Azoarcus sp., Azoarcus sp. 22Lin
-
brenda
Steinbach, A.; Fraas, S.; Harder, J.; Warkentin, E.; Kroneck, P.M.; Ermler, U.
Crystal structure of a ring-cleaving cyclohexane-1,2-dione hydrolase, a novel member of the thiamine diphosphate enzyme family
FEBS J.
279
1209-1219
2012
Azoarcus sp. (P0CH62), Azoarcus sp., Azoarcus sp. 22Lin (P0CH62)
brenda
Steinbach, A.K.; Fraas, S.; Harder, J.; Tabbert, A.; Brinkmann, H.; Meyer, A.; Ermler, U.; Kroneck, P.M.
Cyclohexane-1,2-dione hydrolase from denitrifying Azoarcus sp. strain 22Lin, a novel member of the thiamine diphosphate enzyme family
J. Bacteriol.
193
6760-6769
2011
Azoarcus sp. (P0CH62), Azoarcus sp., Azoarcus sp. 22Lin (P0CH62)
brenda
Loschonsky, S.; Wacker, T.; Waltzer, S.; Giovannini, P.P.; McLeish, M.J.; Andrade, S.L.; Mueller, M.
Extended reaction scope of thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase: from C-C bond cleavage to C-C bond ligation
Angew. Chem. Int. Ed. Engl.
53
14402-14406
2014
Azoarcus sp. (P0CH62), Azoarcus sp. 22Lin (P0CH62)
brenda
Loschonsky, S.; Waltzer, S.; Fraas, S.; Wacker, T.; Andrade, S.L.; Kroneck, P.M.; Mueller, M.
Catalytic scope of the thiamine-dependent multifunctional enzyme cyclohexane-1,2-dione hydrolase
ChemBioChem
15
389-392
2014
Azoarcus sp. (P0CH62), Azoarcus sp. 22Lin (P0CH62)
brenda
Loschonsky, S.; Waltzer, S.; Brecht, V.; Mueller, M.
Elucidation of the enantioselective cyclohexane-1,2-dione hydrolase catalyzed formation of (S)-acetoin
ChemCatChem
6
969-972
2014
Azoarcus sp., Azoarcus sp. 22Lin
-
brenda
Zhu, W.; Liu, Y.
QM/MM study on the catalytic mechanism of cyclohexane-1,2-dione hydrolase (CDH)
Theoret. Chem. Accounts
133
1-9
2014
Azoarcus sp. (P0CH62), Azoarcus sp. 22Lin (P0CH62)
-
brenda