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 | 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 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Azoarcus sp. | P0CH62 | - |
- |
Azoarcus sp. 22Lin | P0CH62 | - |
- |
Purification (Comment) | Organism |
---|---|
native CDH 6.6fold by two different steps of anion exchange chromatography, followed by gel filtration | Azoarcus sp. |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
cyclohexane-1,2-dione + H2O = 6-oxohexanoate | catalytic reaction mechanism, overview | Azoarcus sp. |
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 | 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 | Comment | Organism |
---|---|---|
dimer | 2 * 59000, SDS-PAGE, 2 * 64500, about, sequence calculation | Azoarcus sp. |
Synonyms | Comment | Organism |
---|---|---|
Cdh | - |
Azoarcus sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Azoarcus sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Azoarcus sp. |
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 | 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. |