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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General Information
General Information on EC 3.7.1.11 - cyclohexane-1,2-dione hydrolase
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evolution
metabolism
physiological function
additional information
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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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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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
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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
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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
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physiological function
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thiamine diphosphate-dependent cyclohexane-1,2-dione hydrolase is the key enzyme of an anaerobic degradation pathway of alicyclic alcohols
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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
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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
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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
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additional information
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wild-type and mutant H28A/N484A active site structure analysis, PDB IDs 2PGN and 4D5G
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additional information
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enzyme structure and active site structure analysis from the enzyme-substrate complex crystal structure, PDB ID 2PGN
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