Application | Comment | Organism |
---|---|---|
drug development | the enzyme is a target for antimicrobial and anti-paarasite drugs | Mycobacterium tuberculosis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic analysis and conformational dynamics, overview | Mycobacterium tuberculosis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + shikimate | Mycobacterium tuberculosis | - |
ADP + 3-phosphoshikimate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + shikimate | - |
Mycobacterium tuberculosis | ADP + 3-phosphoshikimate | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme catalyzes the fifth step in the shikimate pathway | Mycobacterium tuberculosis |
physiological function | he phosphate binding domain in the apo-enzyme is fairly rigid and largely protected from solvent access, even at relatively high temperatures. The shikimate binding domain is highly flexible, the apo-enzyme tends to exhibit large conformational changes to permit LID closure after the shikimate binding. The nucleotide binding domain is initially conformationally rigid, which seems to favour the initial orientation of ADP/ATP, but becomes highly flexible at temperatures above 30°C, which may permit domain rotation. Part of the LID domain, including the phosphate binding site, is partially rigid, while another part is highly flexible and accessible to the solvent, mide H/D exchange and mass spectrometry | Mycobacterium tuberculosis |