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Literature summary extracted from
- Purification and characterization of the first archaeal glutamate decarboxylase from Pyrococcus horikoshii (2009), Biosci. Biotechnol. Biochem., 73, 224-227.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.1.1.15 | recombinant expression and sequence comparisons | Pyrococcus horikoshii |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.1.1.15 | additional information | development of a hyperthermostable enzyme for industrial applications, overview | Pyrococcus horikoshii |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.15 | 42000 | - |
1 * 42000, SDS-PAGE | Pyrococcus horikoshii |
| 4.1.1.15 | 43000 | - |
gel filtration | Pyrococcus horikoshii |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.15 | L-glutamate | Pyrococcus horikoshii | - |
4-aminobutanoate + CO2 | - |
ir |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.1.15 | Pyrococcus horikoshii | - |
gene PH0937 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.1.1.15 | recombinant enzyme by ammonium sulfate fractionation, hydrophobic interaction chromatography, and dialysis | Pyrococcus horikoshii |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.15 | L-glutamate | - |
Pyrococcus horikoshii | 4-aminobutanoate + CO2 | - |
ir | |
| 4.1.1.15 | additional information | the recombinant engineered enzyme shows a broad substrate specificity | Pyrococcus horikoshii | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.1.1.15 | monomer | 1 * 42000, SDS-PAGE | Pyrococcus horikoshii |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.1.1.15 | GAD | - |
Pyrococcus horikoshii |
| 4.1.1.15 | More | GAD belongs to a subset of pyridoxal 5'-phosphate-dependent enzymes classified as group 2 | Pyrococcus horikoshii |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.15 | 97 | - |
above, recombinant engineered enzyme | Pyrococcus horikoshii |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.15 | 85 | - |
purified recombinant enzyme, stable | Pyrococcus horikoshii |
| 4.1.1.15 | 95 | - |
purified recombinant enzyme, half-life is 3 h | Pyrococcus horikoshii |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.15 | 8 | - |
recombinant engineered enzyme | Pyrococcus horikoshii |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.1.15 | pyridoxal 5'-phosphate | - |
Pyrococcus horikoshii | |
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Release 2023.1 (January 2023)
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