Crystallization (Comment) | Organism |
---|---|
in complex with glutarate, succinate, and the inhibitor N-oxalyl-glycine | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(S)-2-hydroxyglutarate | weak product inhibition | Escherichia coli | |
N-oxalyl-glycine | - |
Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.1 | - |
2-oxoglutarate | pH 7.2, 30°C | Escherichia coli | |
0.65 | - |
Glutarate | pH 7.2, 30°C | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P76621 | - |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.053 | - |
pH 7.2, 30°C | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glutarate + 2-oxoglutarate + O2 | - |
Escherichia coli | (S)-2-hydroxyglutarate + succinate + CO2 | - |
? | |
additional information | no substrates: oxalate, malonate, succinate, adipate, and pimelate | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
csiD | - |
Escherichia coli |
GlaH | - |
Escherichia coli |
glutarate 2-hydroxylase | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
physiological function | during catabolism of lysine to succinate, CsiD acts as an 2-oxoglutarate-dependent dioxygenase catalysing hydroxylation of glutarate to L-2-hydroxyglutarate. Repression of the pathway by CsiR is relieved upon glutarate binding. In a knockout strain, with carbon starvation and entry into the stationary phase, the intracellular concentration of glutarate accumulates to much higher levels than compared to the wild-type | Escherichia coli |