Any feedback?
Literature summary for 1.1.1.95 extracted from
- A novel mechanism for substrate inhibition in Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase (2007), J. Biol. Chem., 282, 31517-31524.
Protein Variants
| 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
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 3-phosphohydroxypyruvate | uncompetitive substrate inhibition at high substrate concentration | Mycobacterium tuberculosis |  |
KM Value [mM]
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | P9WNX3 | - |
- |
| Mycobacterium tuberculosis H37Rv | P9WNX3 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-phosphohydroxypyruvate + NAD+ | - |
Mycobacterium tuberculosis | ? | - |
r | |
| 3-phosphohydroxypyruvate + NAD+ | - |
Mycobacterium tuberculosis H37Rv | ? | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 3-phosphoglycerate dehydrogenase | - |
Mycobacterium tuberculosis |
Turnover Number [1/s]
| 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
| 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 Range
| 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 [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 | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
