Cloned (Comment) | Organism |
---|---|
mutant enzyme K12G is expressed in Escherichia coli strain DF502 | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
K12G | the mutation results in a ca. 50fold increase in Km for the substrate glyceraldehyde 3-phosphate (GAP) and a 60fold increase in Ki for competitive inhibition by 2-phosphoglycolate, a 12000fold decrease in kcat for isomerization of GAP, and a 6000000fold decrease in kcat/Km for GAP | Saccharomyces cerevisiae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-Phosphoglycolate | competitive inhibition | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.1 | - |
D-glyceraldehyde 3-phosphate | wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C | Saccharomyces cerevisiae | |
50 | - |
D-glyceraldehyde 3-phosphate | mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Purification (Comment) | Organism |
---|---|
DEAE-Sepharose column chromatography | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate | - |
Saccharomyces cerevisiae | dihydroxyacetone phosphate | - |
r |
Synonyms | Comment | Organism |
---|---|---|
TIM | - |
Saccharomyces cerevisiae |
Triosephosphate isomerase | - |
Saccharomyces cerevisiae |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.6 | - |
D-glyceraldehyde 3-phosphate | mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C | Saccharomyces cerevisiae | |
7300 | - |
D-glyceraldehyde 3-phosphate | wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
- |
Saccharomyces cerevisiae |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 8 | - |
Saccharomyces cerevisiae |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.019 | - |
2-Phosphoglycolate | wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C | Saccharomyces cerevisiae | |
1.1 | - |
2-Phosphoglycolate | mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C | Saccharomyces cerevisiae |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.012 | - |
D-glyceraldehyde 3-phosphate | mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C | Saccharomyces cerevisiae | |
6600 | - |
D-glyceraldehyde 3-phosphate | wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C | Saccharomyces cerevisiae |