Application | Comment | Organism |
---|---|---|
drug development | the enzyme can be a target for rational design of specific inhibitors, aiming at the development of antitubercular drugs | Mycobacterium tuberculosis |
Protein Variants | Comment | Organism |
---|---|---|
K69A | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, overview | Mycobacterium tuberculosis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics of wild-type and mutant enzymes, overview | Mycobacterium tuberculosis | |
0.011 | - |
NADPH | wild-type enzyme, pH 7.3, 25°C | Mycobacterium tuberculosis | |
0.029 | - |
3-dehydroshikimate | wild-type enzyme, pH 7.3, 25°C | Mycobacterium tuberculosis | |
0.03 | - |
NADPH | mutant K69A, pH 7.3, 25°C | Mycobacterium tuberculosis | |
0.076 | - |
3-dehydroshikimate | mutant K69A, pH 7.3, 25°C | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-dehydroshikimate + NADPH + H+ | Mycobacterium tuberculosis | - |
shikimate + NADP+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P95001 | gene aroE | - |
no activity in Homo sapiens | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ | catalytic mechanism, residue Lys69 plays a catalytic role and is not involved in substrate binding, overview | Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-dehydroshikimate + NADPH + H+ | - |
Mycobacterium tuberculosis | shikimate + NADP+ | - |
r | |
3-dehydroshikimate + NADPH + H+ | catalytic mechanism, residue Lys69 plays a catalytic role and is not involved in substrate binding | Mycobacterium tuberculosis | shikimate + NADP+ | - |
r |
Subunits | Comment | Organism |
---|---|---|
More | three-dimensional structure analysis of wild-type and mutant enzymes with bound substrates, overview | Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
MtbSD | - |
Mycobacterium tuberculosis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Mycobacterium tuberculosis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.73 | - |
3-dehydroshikimate | mutant K69A, pH 7.3, 25°C | Mycobacterium tuberculosis | |
50 | - |
3-dehydroshikimate | wild-type enzyme, pH 7.3, 25°C | Mycobacterium tuberculosis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.3 | - |
assay at | Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Mycobacterium tuberculosis | |
NADPH | - |
Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
metabolism | aroE-encoded shikimate dehydrogenase catalyzes the forth reaction in the shikimate pathway | Mycobacterium tuberculosis |
additional information | the shikimate pathway is an attractive target for the development of antitubercular agents because it is essential in Mycobacterium tuberculosis, the causative agent of tuberculosis, but absent in humans | Mycobacterium tuberculosis |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
9.6 | - |
3-dehydroshikimate | mutant K69A, pH 7.3, 25°C | Mycobacterium tuberculosis | |
24 | - |
NADPH | mutant K69A, pH 7.3, 25°C | Mycobacterium tuberculosis | |
1700 | - |
3-dehydroshikimate | wild-type enzyme, pH 7.3, 25°C | Mycobacterium tuberculosis | |
4500 | - |
NADPH | wild-type enzyme, pH 7.3, 25°C | Mycobacterium tuberculosis |