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Literature summary for 2.3.3.16 extracted from
- Conversion, by limited proteolysis, of an archaebacterial citrate synthase into essentially a citryl-CoA hydrolase (1992), Eur. J. Biochem., 208, 459-466.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | citrate synthase is converted by limited proteolysis into a citryl-CoA hydrolase. Tryptic hydrolysis occurs at the N-terminal region of citrate synthase. The peptide removed from the enzyme by trypsin contains less than about 15 amino acid residues | Saccharolobus solfataricus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | limited proteolysis of citrate synthase from Sulfolobus solfataricus by trypsin reduces the rate of the overall reaction (acetyl-CoA + oxaloacetate + H2O -> citrate + CoASH) to 4% but does not affect the hydrolysis of citryl-CoA. A connecting link between the enzyme's ligase and hydrolase activity becomes impaired specifically on treatment with trypsin. Other proteolytic enzymes like chymotrypsin and subtilisin inactivate catalytic functions of citrate synthase, ligase and hydrolase, equally well | Saccharolobus solfataricus | |
| S-carboxymethyl-CoA | competitive inhibition versus acetyl-CoA, non-competitive inhibition versus oxaloacetate; inhibits the native enzyme competitively versus acetyl-CoA and non-competitively versus oxaloacetate | Saccharolobus solfataricus |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0075 | - |
acetyl-CoA | pH and temperature not specified in the publication | Saccharolobus solfataricus | |
| 0.0075 | - |
acetyl-CoA | 25°C, pH and temperature not specified in the publication | Saccharolobus solfataricus | |
| 0.0183 | - |
oxaloacetate | pH and temperature not specified in the publication | Saccharolobus solfataricus | |
| 0.0183 | - |
oxaloacetate | 25°C, pH and temperature not specified in the publication | Saccharolobus solfataricus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | - |
- |
- |
| Saccharolobus solfataricus | P80148 | - |
- |
| Saccharolobus solfataricus P1 | - |
- |
- |
| Saccharolobus solfataricus P2 | P80148 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Saccharolobus solfataricus |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -20°C, 7-10 mg/ml, 50 mM Tris buffer, pH 8.0, stable for at least 1 year | Saccharolobus solfataricus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + H2O + oxaloacetate | limited proteolysis of citrate synthase from Sulfolobus solfataricus by trypsin reduces the rate of the overall reaction (acetyl-CoA + oxaloacetate + H2O -> citrate + CoASH) to 4% but does not affect the hydrolysis of citryl-CoA. A connecting link between the enzyme's ligase and hydrolase activity becomes impaired specifically on treatment with trypsin. Other proteolytic enzymes like chymotrypsin and subtilisin inactivate catalytic functions of citrate synthase, ligase and hydrolase, equally well | Saccharolobus solfataricus | citrate + CoA | - |
? | |
| acetyl-CoA + H2O + oxaloacetate | the activity with propanoyl-CoA is not tested | Saccharolobus solfataricus | citrate + CoA | - |
? | |
| acetyl-CoA + H2O + oxaloacetate | the activity with propanoyl-CoA is not tested | Saccharolobus solfataricus P2 | citrate + CoA | - |
? | |
| acetyl-CoA + H2O + oxaloacetate | limited proteolysis of citrate synthase from Sulfolobus solfataricus by trypsin reduces the rate of the overall reaction (acetyl-CoA + oxaloacetate + H2O -> citrate + CoASH) to 4% but does not affect the hydrolysis of citryl-CoA. A connecting link between the enzyme's ligase and hydrolase activity becomes impaired specifically on treatment with trypsin. Other proteolytic enzymes like chymotrypsin and subtilisin inactivate catalytic functions of citrate synthase, ligase and hydrolase, equally well | Saccharolobus solfataricus P1 | citrate + CoA | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | - |
Saccharolobus solfataricus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SSO2589 | locus name | Saccharolobus solfataricus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Saccharolobus solfataricus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 6 | - |
Saccharolobus solfataricus |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00037 | - |
S-carboxymethyl-CoA | 25°C, pH and temperature not specified in the publication, competitive inhibition versus acetyl-CoA | Saccharolobus solfataricus | |
| 0.00037 | - |
S-carboxymethyl-CoA | pH and temperature not specified in the publication, competitively inhibition versus acetyl-CoA | Saccharolobus solfataricus | |
| 0.0024 | - |
S-carboxymethyl-CoA | 25°C, pH and temperature not specified in the publication, non-competitive inhibition versus oxaloacetate | Saccharolobus solfataricus | |
| 0.0024 | - |
S-carboxymethyl-CoA | non-competitively inhibition versus oxaloacetate, pH and temperature not specified in the publication | Saccharolobus solfataricus | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Saccharolobus solfataricus | isoelectric focusing, pH-range 5.5-8.5, 10°C, native citrate synthase | - |
6.7 |
| Saccharolobus solfataricus | native citrate synthase | - |
6.7 |
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