Cloned (Comment) | Organism |
---|---|
- |
Oryctolagus cuniculus |
expression in Saccharomyces cerevsiae | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
structure of TPI with bound phosphoenolpyruvate at 1.6 A resolution. Phosphoenolpyruvate is bound to the catalytic pocket of TPI and occludes substrate | Oryctolagus cuniculus |
Protein Variants | Comment | Organism |
---|---|---|
I170T | 13% residual activity | Homo sapiens |
I170V | 5.9% residual activity | Homo sapiens |
K13R | mutant is catalytically inactive and largely unstable | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
phosphoenolpyruvate | competitive | Homo sapiens | |
phosphoenolpyruvate | competitive | Oryctolagus cuniculus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.303 | - |
D-glyceraldehyde 3-phosphate | mutant I170T, pH not specified in the publication, temperature not specified in the publication | Homo sapiens | |
0.687 | - |
D-glyceraldehyde 3-phosphate | mutant I170V, pH not specified in the publication, temperature not specified in the publication | Homo sapiens | |
1.373 | - |
D-glyceraldehyde 3-phosphate | wild-type, pH not specified in the publication, temperature not specified in the publication | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Oryctolagus cuniculus | P00939 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate | - |
Homo sapiens | dihydroxyacetone 3-phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
TpI | - |
Homo sapiens |
TpI | - |
Oryctolagus cuniculus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.2 | - |
phosphoenolpyruvate | mutant I170T, pH not specified in the publication, temperature not specified in the publication | Homo sapiens | |
0.23 | - |
phosphoenolpyruvate | wild-type, pH not specified in the publication, temperature not specified in the publication | Homo sapiens | |
0.5 | - |
phosphoenolpyruvate | mutant I170V, pH not specified in the publication, temperature not specified in the publication | Homo sapiens |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.154 | - |
mutant I170T, pH not specified in the publication, temperature not specified in the publication | Homo sapiens | phosphoenolpyruvate | |
0.193 | - |
mutant I170V, pH not specified in the publication, temperature not specified in the publication | Homo sapiens | phosphoenolpyruvate | |
0.57 | - |
wild-type, pH not specified in the publication, temperature not specified in the publication | Homo sapiens | phosphoenolpyruvate |
General Information | Comment | Organism |
---|---|---|
physiological function | glycolytic regulation requires direct catalytic inhibition of TPI by the pyruvate kinase substrate phosphoenolpyruvate | Oryctolagus cuniculus |
physiological function | transgenic yeast cells expressing mutations I170V or I170T accumulate greater levels of pentose phosphate pathway intermediates and have altered stress resistance, mimicking the activation of the pyruvate kinase-TPI feedback loop. Glycolytic regulation requires direct catalytic inhibition of TPI by the pyruvate kinase substrate phosphoenolpyruvate | Homo sapiens |