Cloned (Comment) | Organism |
---|---|
overexpressed in Escherichia coli | Archaeoglobus fulgidus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-tyrosine | 0.5 mM, 50% inhibition | Archaeoglobus fulgidus | |
additional information | phenylalanine (up to 5 mM) has no effect. Not inhibited by prephenate or NAD+ at concentrations up to 10 and 2 mM, respectively | Archaeoglobus fulgidus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.047 | - |
NAD+ | pH 6.5, 87°C | Archaeoglobus fulgidus | |
0.45 | - |
prephenate | pH 6.5, 87°C | Archaeoglobus fulgidus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
66000 | - |
6 * 66000, SDS-PAGE | Archaeoglobus fulgidus |
70946 | - |
6 * 70946, calculated from sequence | Archaeoglobus fulgidus |
420000 | - |
gel filtration | Archaeoglobus fulgidus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
prephenate + NAD+ | Archaeoglobus fulgidus | the enzyme is involved in aromatic amino acid biosynthesis | 4-hydroxyphenylpyruvate + CO2 + NADH | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Archaeoglobus fulgidus | O30012 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Archaeoglobus fulgidus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
prephenate + NAD+ | the enzyme is involved in aromatic amino acid biosynthesis | Archaeoglobus fulgidus | 4-hydroxyphenylpyruvate + CO2 + NADH | - |
? | |
prephenate + NAD+ | activity with NADP+ as coenzyme is about 10% of that with NAD+, suggesting that NAD+ is likely the preferred and physiological coenzyme | Archaeoglobus fulgidus | 4-hydroxyphenylpyruvate + CO2 + NADH | - |
? |
Subunits | Comment | Organism |
---|---|---|
homohexamer | 6 * 66000, SDS-PAGE | Archaeoglobus fulgidus |
homohexamer | 6 * 70946, calculated from sequence | Archaeoglobus fulgidus |
Synonyms | Comment | Organism |
---|---|---|
AroQ | gene name. Trifunctional enzyme EC 5.4.99.5 (chorismate mutase)/EC 4.2.1.51 (prephenate dehydratase)/EC 1.3.1.12 (prephenate dehydrogenase) | Archaeoglobus fulgidus |
CM/PDT/PDHG | trifunctional enzyme EC 5.4.99.5 (chorismate mutase)/EC 4.2.1.51 (prephenate dehydratase)/EC 1.3.1.12 (prephenate dehydrogenase) | Archaeoglobus fulgidus |
PDHG | - |
Archaeoglobus fulgidus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
87 | - |
assay at | Archaeoglobus fulgidus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | activity with NADP+ as coenzyme is about 10% of that with NAD+, suggesting that NAD+ is likely the preferred and physiological coenzyme | Archaeoglobus fulgidus |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme is involved in aromatic amino acid biosynthesis | Archaeoglobus fulgidus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
880 | - |
prephenate | pH 6,5, 87°C | Archaeoglobus fulgidus |