3.7.1.11: cyclohexane-1,2-dione hydrolase
This is an abbreviated version!
For detailed information about cyclohexane-1,2-dione hydrolase, go to the full flat file.
Reaction
Synonyms
Cdh, ThDP-dependent cyclohexane-1,2-dione hydrolase, thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase
ECTree
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Substrates Products
Substrates Products on EC 3.7.1.11 - cyclohexane-1,2-dione hydrolase
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REACTION DIAGRAM
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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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
-
-
?
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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-
?
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 + ?
-
further convertion 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
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?
?
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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
?
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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
-
-
?
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
-
-
?
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
-
-
?