Literature summary 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.
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.7.1.11 |
Cyclohexane-1,2-dione |
substrate inhibition above 0.1 mM |
Azoarcus sp. |
|
3.7.1.11 |
additional information |
activity decreases significantly at this high ionic strength |
Azoarcus sp. |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.7.1.11 |
Mg2+ |
1.0 Mg2+ molecule per enzyme monomer |
Azoarcus sp. |
|
3.7.1.11 |
additional information |
activity decreases significantly at this high ionic strength |
Azoarcus sp. |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
3.7.1.11 |
59000 |
- |
2 * 59000, SDS-PAGE, 2 * 64500, about, sequence calculation |
Azoarcus sp. |
3.7.1.11 |
64500 |
- |
2 * 59000, SDS-PAGE, 2 * 64500, about, sequence calculation |
Azoarcus sp. |
3.7.1.11 |
105000 |
- |
gel filtration |
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. |
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 |
? |
|
3.7.1.11 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.7.1.11 |
Azoarcus sp. |
P0CH62 |
- |
- |
3.7.1.11 |
Azoarcus sp. 22Lin |
P0CH62 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.7.1.11 |
native CDH 6.6fold by two different steps of anion exchange chromatography, followed by gel filtration |
Azoarcus sp. |
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. |
|
Specific Activity [micromol/min/mg]
EC Number |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
---|
3.7.1.11 |
0.677 |
- |
purified enzyme, pH 8.0, 37°C |
Azoarcus sp. |
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 convertion to adipate using NAD+ as electron acceptor |
? |
|
3.7.1.11 |
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 |
? |
|
3.7.1.11 |
cyclohexane-1,2-dione + H2O |
- |
Azoarcus sp. 22Lin |
6-oxohexanoate + ? |
further convertion to adipate using NAD+ as electron acceptor |
? |
|
3.7.1.11 |
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
EC Number |
Subunits |
Comment |
Organism |
---|
3.7.1.11 |
dimer |
2 * 59000, SDS-PAGE, 2 * 64500, about, sequence calculation |
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. |
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 |
1.0 FAD molecule per enzyme monomer, 2fold Rossmann fold for FAD binding at the C-terminal end |
Azoarcus sp. |
|
3.7.1.11 |
thiamine diphosphate |
dependent on, 0.8 ThDP per enzyme monomer, ThDP binding motif, overview |
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 |
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. |