Protein Variants | Comment | Organism |
---|---|---|
H447A | anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.16, kcat: 1446, Ki (mM) (3-phosphohydroxypyruvate): 0.87, mutant displays complete uncompetitive substrate inhibition, no dual pH optima compared to wild-type | Mycobacterium tuberculosis |
K439A | anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.075, kcat: 368, Ki (mM) (3-phosphohydroxypyruvate): 0.054, mutant displays partial uncompetitive substrate inhibition, mutant retains dual pH optima | Mycobacterium tuberculosis |
R446A | anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.123 kcat: 467, Ki (mM) (3-phosphohydroxypyruvate): 0.289, mutant displays partial uncompetitive substrate inhibition, no dual pH optima compared to wild-type | Mycobacterium tuberculosis |
R451A | anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.19, kcat: 1881, Ki (mM) (3-phosphohydroxypyruvate): 0.95, mutant displays complete uncompetitive substrate inhibition, no dual pH optima compared to wild-type | Mycobacterium tuberculosis |
R501A | anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.18, kcat: 1989, Ki (mM) (3-phosphohydroxypyruvate): 1.02, mutant displays complete uncompetitive substrate inhibition, no dual pH optima compared to wild-type | Mycobacterium tuberculosis |
R501A/R451A/K439A | anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.243, kcat: 1558, Ki (mM) (3-phosphohydroxypyruvate): 7.218, mutant displays only little uncompetitive substrate inhibition, no dual pH optima compared to wild-type | Mycobacterium tuberculosis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
3-phosphohydroxypyruvate | uncompetitive substrate inhibition at high substrate concentration | Mycobacterium tuberculosis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.075 | - |
3-phosphohydroxypyruvate | mutant K439A | Mycobacterium tuberculosis | |
0.123 | - |
3-phosphohydroxypyruvate | mutant R446A | Mycobacterium tuberculosis | |
0.16 | - |
3-phosphohydroxypyruvate | mutant H447A | Mycobacterium tuberculosis | |
0.17 | - |
3-phosphohydroxypyruvate | - |
Mycobacterium tuberculosis | |
0.18 | - |
3-phosphohydroxypyruvate | mutant R501A | Mycobacterium tuberculosis | |
0.19 | - |
3-phosphohydroxypyruvate | mutant R451A | Mycobacterium tuberculosis | |
0.243 | - |
3-phosphohydroxypyruvate | mutant R501A/R451A/K439A | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WNX3 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WNX3 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-phosphohydroxypyruvate + NAD+ | - |
Mycobacterium tuberculosis | ? | - |
r | |
3-phosphohydroxypyruvate + NAD+ | - |
Mycobacterium tuberculosis H37Rv | ? | - |
r |
Synonyms | Comment | Organism |
---|---|---|
3-phosphoglycerate dehydrogenase | - |
Mycobacterium tuberculosis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
368 | - |
3-phosphohydroxypyruvate | mutant K439A | Mycobacterium tuberculosis | |
467 | - |
3-phosphohydroxypyruvate | mutant R446A | Mycobacterium tuberculosis | |
1446 | - |
3-phosphohydroxypyruvate | mutant H447A | Mycobacterium tuberculosis | |
1558 | - |
3-phosphohydroxypyruvate | mutant R501A/R451A/K439A | Mycobacterium tuberculosis | |
1881 | - |
3-phosphohydroxypyruvate | mutant R451A | Mycobacterium tuberculosis | |
1989 | - |
3-phosphohydroxypyruvate | mutant R501A | Mycobacterium tuberculosis | |
2461 | - |
3-phosphohydroxypyruvate | - |
Mycobacterium tuberculosis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.2 | - |
enzyme possess a dual pH optimum. A significant decrease in the Ki for substrate inhibition at pH values corresponding to the valley between these optima is responsible for this phenomenon | Mycobacterium tuberculosis |
8 | - |
enzyme possess a dual pH optimum. A significant decrease in the Ki for substrate inhibition at pH values corresponding to the valley between these optima is responsible for this phenomenon | Mycobacterium tuberculosis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5.2 | 5.7 | at approximately pH 5.7 the activity starts increasing again and reaches a new optimum at approximately pH 5.2 before decreasing once again | Mycobacterium tuberculosis |
7.5 | 9.5 | activity is relatively constant between pH 7.5-9.5. Above pH 9.5 and below pH 7.5 activity falls off rapidly | Mycobacterium tuberculosis |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.054 | - |
3-phosphohydroxypyruvate | mutant K439A | Mycobacterium tuberculosis | |
0.289 | - |
3-phosphohydroxypyruvate | mutant R446A | Mycobacterium tuberculosis | |
0.87 | - |
3-phosphohydroxypyruvate | mutant H447A | Mycobacterium tuberculosis | |
0.95 | - |
3-phosphohydroxypyruvate | - |
Mycobacterium tuberculosis | |
0.95 | - |
3-phosphohydroxypyruvate | mutant R451A | Mycobacterium tuberculosis | |
1.02 | - |
3-phosphohydroxypyruvate | mutant R501A | Mycobacterium tuberculosis | |
7.218 | - |
3-phosphohydroxypyruvate | mutant R501A/R451A/K439A | Mycobacterium tuberculosis |