Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.7.1.11 extracted from

  • 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 (2011), J. Bacteriol., 193, 6760-6769.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.7.1.11

Inhibitors

Inhibitors Comment Organism Structure
Cyclohexane-1,2-dione substrate inhibition above 0.1 mM Azoarcus sp.
additional information activity decreases significantly at this high ionic strength Azoarcus sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ 1.0 Mg2+ molecule per enzyme monomer Azoarcus sp.
additional information activity decreases significantly at this high ionic strength Azoarcus sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
59000
-
 2 * 59000, SDS-PAGE, 2 * 64500, about, sequence calculation Azoarcus sp.
64500
-
 2 * 59000, SDS-PAGE, 2 * 64500, about, sequence calculation Azoarcus sp.
105000
-
 gel filtration 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. 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 6-oxohexanoate + ? further convertion to adipate using NAD+ as electron acceptor ?
cyclohexane-1,2-dione + H2O Azoarcus sp. 22Lin 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 6-oxohexanoate + ? further convertion to adipate using NAD+ as electron acceptor ?

Organism

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

Purification (Commentary)

Purification (Comment) Organism
native CDH 6.6fold by two different steps of anion exchange chromatography, followed by gel filtration Azoarcus sp.

Reaction

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.677
-
 purified enzyme, pH 8.0, 37°C Azoarcus sp.

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 59000, SDS-PAGE, 2 * 64500, about, sequence calculation Azoarcus sp.

Synonyms

Synonyms Comment Organism
Cdh
-
 Azoarcus sp.

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
FAD 1.0 FAD molecule per enzyme monomer, 2fold Rossmann fold for FAD binding at the C-terminal end Azoarcus sp.
thiamine diphosphate dependent on, 0.8 ThDP per enzyme monomer, ThDP binding motif, overview Azoarcus sp.

General Information

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