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Literature summary extracted from
- Characterization of two key enzymes for aromatic amino acid biosynthesis in symbiotic archaea (2016), Extremophiles, 20, 503-514.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.3.1.13 | expressed in Escherichia coli BL21(DE3) cells | Nanoarchaeum equitans |
| 1.3.1.13 | expressed in Escherichia coli BL21(DE3) cells | Ignicoccus hospitalis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.1.13 | additional information | not inhibited by L-Tyr | Ignicoccus hospitalis | |
| 1.3.1.13 | additional information | not inhibited by L-Tyr | Nanoarchaeum equitans |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.3.1.13 | 0.062 | - |
NADP+ | at pH 8.0 and 80°C | Ignicoccus hospitalis |  |
| 1.3.1.13 | 0.319 | - |
prephenate | with NAD+ as cosubstrate, at pH 8.0 and 80°C | Ignicoccus hospitalis | |
| 1.3.1.13 | 0.36 | - |
NADP+ | at pH 8.0 and 80°C | Nanoarchaeum equitans | |
| 1.3.1.13 | 0.443 | - |
prephenate | with NADP+ as cosubstrate, at pH 8.0 and 80°C | Ignicoccus hospitalis | |
| 1.3.1.13 | 0.561 | - |
NAD+ | at pH 8.0 and 80°C | Ignicoccus hospitalis | |
| 1.3.1.13 | 0.69 | - |
prephenate | with NAD+ as cosubstrate, at pH 8.0 and 80°C | Nanoarchaeum equitans | |
| 1.3.1.13 | 0.73 | - |
prephenate | with NADP+ as cosubstrate, at pH 8.0 and 80°C | Nanoarchaeum equitans | |
| 1.3.1.13 | 3.3 | - |
NAD+ | at pH 8.0 and 80°C | Nanoarchaeum equitans | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.3.1.13 | 71000 | - |
analytical ultracentrifugation | Nanoarchaeum equitans |
| 1.3.1.13 | 85000 | - |
analytical ultracentrifugation | Ignicoccus hospitalis |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.1.13 | prephenate + NAD+ | Nanoarchaeum equitans | - |
4-hydroxyphenylpyruvate + CO2 + NADH | - |
? | |
| 1.3.1.13 | prephenate + NAD+ | Ignicoccus hospitalis | - |
4-hydroxyphenylpyruvate + CO2 + NADH | - |
? | |
| 1.3.1.13 | prephenate + NADP+ | Nanoarchaeum equitans | the enzyme prefers NADP+ over NAD+ | 4-hydroxyphenylpyruvate + CO2 + NADPH | - |
? | |
| 1.3.1.13 | prephenate + NADP+ | Ignicoccus hospitalis | the enzyme prefers NADP+ over NAD+ | 4-hydroxyphenylpyruvate + CO2 + NADPH | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.3.1.13 | Ignicoccus hospitalis | A8AAX2 | - |
- |
| 1.3.1.13 | Nanoarchaeum equitans | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.3.1.13 | Ni-NTA column chromatography, and Superdex 200 gel filtration | Nanoarchaeum equitans |
| 1.3.1.13 | Ni-NTA column chromatography, and Superdex 200 gel filtration | Ignicoccus hospitalis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.1.13 | prephenate + NAD+ | - |
Nanoarchaeum equitans | 4-hydroxyphenylpyruvate + CO2 + NADH | - |
? | |
| 1.3.1.13 | prephenate + NAD+ | - |
Ignicoccus hospitalis | 4-hydroxyphenylpyruvate + CO2 + NADH | - |
? | |
| 1.3.1.13 | prephenate + NADP+ | the enzyme prefers NADP+ over NAD+ | Nanoarchaeum equitans | 4-hydroxyphenylpyruvate + CO2 + NADPH | - |
? | |
| 1.3.1.13 | prephenate + NADP+ | the enzyme prefers NADP+ over NAD+ | Ignicoccus hospitalis | 4-hydroxyphenylpyruvate + CO2 + NADPH | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.3.1.13 | homodimer | - |
Nanoarchaeum equitans |
| 1.3.1.13 | homodimer | - |
Ignicoccus hospitalis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.3.1.13 | CM-PD | bifunctional enzyme with chorismate mutase and prephenate dehydrogenase activities | Ignicoccus hospitalis |
| 1.3.1.13 | PD-CM-PDT | trifunctional enzyme with chorismate mutase, prephenate dehydrogenase and prephenate dehydratase activities | Nanoarchaeum equitans |
| 1.3.1.13 | tyrA | - |
Nanoarchaeum equitans |
| 1.3.1.13 | tyrA | - |
Ignicoccus hospitalis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.3.1.13 | 90 | - |
- |
Nanoarchaeum equitans |
| 1.3.1.13 | 90 | - |
- |
Ignicoccus hospitalis |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.3.1.13 | 80 | 95 | the enzyme retains full dehydrogenase activity after 50 h incubation at 80°C and greater than 50% of specific activity after 50 h at 95°C | Nanoarchaeum equitans |
| 1.3.1.13 | 80 | 95 | the enzyme retains full dehydrogenase activity after 50 h incubation at 80°C and greater than 50% of specific activity after 50 h at 95°C | Ignicoccus hospitalis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.1.13 | NAD+ | - |
Nanoarchaeum equitans | |
| 1.3.1.13 | NAD+ | - |
Ignicoccus hospitalis | |
| 1.3.1.13 | NADP+ | the enzyme prefers NADP+ over NAD+ | Nanoarchaeum equitans | |
| 1.3.1.13 | NADP+ | the enzyme prefers NADP+ over NAD+ | Ignicoccus hospitalis | |
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Release 2023.1 (January 2023)
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