Crystallization (Comment) | Organism |
---|---|
structure of a ternary complex with NAD+ and tyrosine to 2.2 A resolution, a binary complex with tyrosine, and a structure of an isolated ACT domain dimer | Bacillus anthracis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-tyrosine | tyrosine binding to ACT domains inactivates the enzyme by blocking both substrate-binding sites and one NAD+ site with the ACT domain of one subunit. Interaction occurs with residues S333 and D315 for both ACT domains | Bacillus anthracis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.045 | - |
prephenate | presence of 0.002 mM L-tyrosine, pH 7.5, 25°C | Bacillus anthracis | |
0.056 | - |
prephenate | presence of 0.006 mM L-tyrosine, pH 7.5, 25°C | Bacillus anthracis | |
0.057 | - |
prephenate | pH 7.5, 25°C | Bacillus anthracis | |
0.237 | - |
NAD+ | pH 7.5, 25°C | Bacillus anthracis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus anthracis | Q81P63 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
prephenate + NAD+ | - |
Bacillus anthracis | 4-hydroxyphenylpyruvate + CO2 + NADH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
tyrA | - |
Bacillus anthracis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
presence of NAD+, NADH, NADP+, and NADPH does not significantly change the melting temperature | Bacillus anthracis |
41 | - |
melting temperature | Bacillus anthracis |
51 | - |
melting temperature, presence of 10 mM L-tyrosine | Bacillus anthracis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3.5 | - |
prephenate | presence of 0.006mM L-tyrosine, pH 7.5, 25°C | Bacillus anthracis | |
12.3 | - |
prephenate | presence of 0.002 mM L-tyrosine, pH 7.5, 25°C | Bacillus anthracis | |
49 | - |
prephenate | pH 7.5, 25°C | Bacillus anthracis |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0015 | - |
L-tyrosine | pH 7.5, 25°C | Bacillus anthracis |
General Information | Comment | Organism |
---|---|---|
physiological function | PDH is allosterically regulated by tyrosine binding to the ACT domains, resulting in an asymmetric conformation of the DPH dimer that sterically prevents prephenate binding to either active site | Bacillus anthracis |