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Literature summary extracted from

  • 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 (2012), FEBS J., 279, 1209-1219.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.7.1.11 thiamine diphosphate dependent on, one molecule ThDP per enzyme monomer Azoarcus sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.7.1.11 purified CDH from strain 22Lin, hanging drop vapour diffusion method, equal volumes of protein storage and reservoir solution, the latter composed of 60% MPD, 20 mM Na+ acetate and 200 mM NaCl, 25°C, a second cubic crystal form is obtained at 20°C with a reservoir solution containing 17-18% w/v PEG 8000, 100 mM Na+ acetate, 10 mM MnCl2, and 2% w/v isopropanol in 0.1 M HEPES buffer, pH 7.5, X-ray diffraction structure determination and analysis at 1.26 A resolution, modeling Azoarcus sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.7.1.11 2-methyl-2,4-pentane-diol MPD, competitive inhibitor, shows selective binding to the open funnel of CDH and strong binding to the active site. It contacts besides GlyA399 the apolar side chains of PheA259, TrpA285, LeuA551, LeuA487 and LeuA563 Azoarcus sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.7.1.11 additional information
-
 additional information CDH follows Michaelis-Menten kinetics Azoarcus sp.
3.7.1.11 0.0133
-
 Cyclohexane-1,2-dione pH 8.0, 37°C Azoarcus sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.7.1.11 Mg2+ one Mg2+ molecule per enzyme monomer Azoarcus sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.7.1.11 cyclohexane-1,2-dione + H2O Azoarcus sp.
-
 6-oxohexanoate + ? further conversion to adipate using NAD+ as electron acceptor ?
3.7.1.11 cyclohexane-1,2-dione + H2O Azoarcus sp. 22Lin
-
 6-oxohexanoate + ? further conversion to adipate using NAD+ as electron acceptor ?

Organism

EC Number Organism UniProt Comment Textmining
3.7.1.11 Azoarcus sp. P0CH62
-
-
3.7.1.11 Azoarcus sp. 22Lin P0CH62
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.7.1.11 cyclohexane-1,2-dione + H2O = 6-oxohexanoate catalytic reaction mechanism, overview Azoarcus sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.7.1.11 cyclohexane-1,2-dione + H2O
-
 Azoarcus sp. 6-oxohexanoate + ? further conversion to adipate using NAD+ as electron acceptor ?
3.7.1.11 cyclohexane-1,2-dione + H2O
-
 Azoarcus sp. 22Lin 6-oxohexanoate + ? further conversion to adipate using NAD+ as electron acceptor ?

Subunits

EC Number Subunits Comment Organism
3.7.1.11 tetramer
-
 Azoarcus sp.

Synonyms

EC Number Synonyms Comment Organism
3.7.1.11 Cdh
-
 Azoarcus sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.7.1.11 37
-
 assay at Azoarcus sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.7.1.11 1.6
-
 Cyclohexane-1,2-dione pH 8.0, 37°C Azoarcus sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.7.1.11 8
-
 assay at Azoarcus sp.

Cofactor

EC Number Cofactor Comment Organism Structure
3.7.1.11 FAD flavoenzyme, the redox-active cofactor FAD seems not to participate in catalysis, one FAD molecule per enzyme monomer. The FAD cofactor is bound in an extended conformation at the C-terminal end of the six-stranded betab-sheet of the domain beta Azoarcus sp.

General Information

EC Number General Information Comment Organism
3.7.1.11 evolution the ring-cleaving cyclohexane-1,2-dione hydrolase is a member of the thiamine diphosphate enzyme family Azoarcus sp.
3.7.1.11 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 Azoarcus sp.
3.7.1.11 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 Azoarcus sp.

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.7.1.11 0.0012
-
 Cyclohexane-1,2-dione pH 8.0, 37°C Azoarcus sp.