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Literature summary for 4.2.1.51 extracted from
- Characterization of a key trifunctional enzyme for aromatic amino acid biosynthesis in Archaeoglobus fulgidus (2009), Extremophiles, 13, 191-198.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| L-tyrosine | enzyme activation by 70% at 1 mM | Archaeoglobus fulgidus |  |
| Tyr | 1 mM, 70% increase in activity | Archaeoglobus fulgidus | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli (DE3)-RIL, pIS85 expression plasmid | Archaeoglobus fulgidus |
| overexpressed in Escherichia coli | Archaeoglobus fulgidus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| L-phenylalanine | inhibits activity at 5 microM, competitive inhibition | Archaeoglobus fulgidus | |
| Phe | 0.005 mM, 66% inhibition, competitive with prephenate | Archaeoglobus fulgidus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.3 | - |
phenylpyruvate | measuring the appearance of phenylpyruvate at 320 nm, performed with 1 mM prephenate in 200 mM Tris buffer | Archaeoglobus fulgidus | |
| 1.3 | - |
prephenate | 77°C, pH not specified in the publication | Archaeoglobus fulgidus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 66000 | - |
trifunctional enzyme, SDS-PAGE | Archaeoglobus fulgidus |
| 70946 | - |
6 * 70946, calculated from sequence | Archaeoglobus fulgidus |
| 70950 | - |
calculated by sequence | Archaeoglobus fulgidus |
| 420000 | - |
gel filtration | Archaeoglobus fulgidus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| prephenate | Archaeoglobus fulgidus | the enzyme is involved in aromatic amino acid biosynthesis | phenylpyruvate + H2O + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Archaeoglobus fulgidus | O30012 | - |
- |
| Nanoarchaeum equitans | Q74NC4 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Archaeoglobus fulgidus |
| gel filtration | Archaeoglobus fulgidus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
trifunctional enzyme containing prephenate dehydratase (PDT), also chorismate mutase (CM, 5.4.99.5), and prephenate dehydrogenase (PDHG, 1.3.1.12) acitivities | Nanoarchaeum equitans |
| additional information | - |
trifunctional enzyme containing prephenate dehydratase (PDT), also chorismate mutase (CM, 5.4.99.5), and prephenate dehydrogenase (PDHG, 1.3.1.12) acitivities, prephenate dehydratase activity spectrophotometric quantified by monitoring the appearance of phenylpyruvate at 320 nm in end-point assays | Archaeoglobus fulgidus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| prephenate | - |
Archaeoglobus fulgidus | phenylpyruvate + H2O + CO2 | - |
? | |
| prephenate | prephenate dehydratase part of trifunctional enzyme | Nanoarchaeum equitans | phenylpyruvate + H2O + CO2 | - |
? | |
| prephenate | spectrophotometric assay by measuring the appearance of phenylpyruvate | Archaeoglobus fulgidus | phenylpyruvate + H2O + CO2 | - |
? | |
| prephenate | the enzyme is involved in aromatic amino acid biosynthesis | Archaeoglobus fulgidus | phenylpyruvate + H2O + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homohexamer | 6 * 66000, SDS-PAGE | Archaeoglobus fulgidus |
| homohexamer | trifunctional enzyme, SDS-PAGE | Archaeoglobus fulgidus |
| homohexamer | 6 * 70946, calculated from sequence | Archaeoglobus fulgidus |
Synonyms
| 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 |
| PDT | - |
Archaeoglobus fulgidus |
| PDT protein | - |
Archaeoglobus fulgidus |
| PDT protein | - |
Nanoarchaeum equitans |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 77 | - |
assay at | Archaeoglobus fulgidus |
| 77 | - |
spectrophotometric assay at | Archaeoglobus fulgidus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | 9.5 | spectrophotometric assay performed at several different pH values | Archaeoglobus fulgidus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the enzyme is involved in aromatic amino acid biosynthesis | Archaeoglobus fulgidus |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.78 | - |
prephenate | 77°C, pH not specified in the publication | Archaeoglobus fulgidus | |
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