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Literature summary for 3.7.1.11 extracted from

  • Zhu, W.; Liu, Y.
    QM/MM study on the catalytic mechanism of cyclohexane-1,2-dione hydrolase (CDH) (2014), Theoret. Chem. Accounts, 133, 1-9.
No PubMed abstract available
Search for more literature for 3.7.1.11

Application

Application Comment Organism
degradation the enzyme is involved in biodegradation of alicyclic compounds involving a C-C bond ring cleavage to generate an aliphatic intermediate. Alicyclic alcohols compounds, which can serve as insecticides, herbicides, or as intermediates and solvents in chemical industries, are widespread in nature as the secondary metabolites of plant and occurring in fossil fuels Azoarcus sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis of CDH in complex with substrate cyclohexane-1,2-dione, PDB ID 2PGN Azoarcus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cyclohexane-1,2-dione + H2O Azoarcus sp.
-
 6-oxohexanoate
-
 ?
cyclohexane-1,2-dione + H2O Azoarcus sp. 22Lin
-
 6-oxohexanoate
-
 ?

Organism

Organism UniProt Comment Textmining
Azoarcus sp. P0CH62
-
-
Azoarcus sp. 22Lin P0CH62
-
-

Reaction

Reaction Comment Organism Reaction ID
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 Azoarcus sp.
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclohexane-1,2-dione + H2O
-
 Azoarcus sp. 6-oxohexanoate
-
 ?
cyclohexane-1,2-dione + H2O 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 Azoarcus sp. 6-oxohexanoate
-
 ?
cyclohexane-1,2-dione + H2O
-
 Azoarcus sp. 22Lin 6-oxohexanoate
-
 ?
cyclohexane-1,2-dione + H2O 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 Azoarcus sp. 22Lin 6-oxohexanoate
-
 ?
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 Azoarcus sp. ?
-
 ?
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 Azoarcus sp. 22Lin ?
-
 ?

Synonyms

Synonyms Comment Organism
Cdh
-
 Azoarcus sp.

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate dependent on Azoarcus sp.

General Information

General Information Comment Organism
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 Azoarcus sp.
additional information enzyme structure and active site structure analysis from the enzyme-substrate complex crystal structure, PDB ID 2PGN Azoarcus sp.