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Literature summary extracted from
- Expression and functional analysis of glutamate synthase small subunit-like proteins from archaeon Pyrococcus horikoshii (2011), Microbiol. Res., 166, 294-303.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.4.1.13 | gene PH0876, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli strain Rosetta (DE3) | Pyrococcus horikoshii |
| 1.4.1.13 | gene PH1873, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli strain Rosetta (DE3) | Pyrococcus horikoshii |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.4.1.13 | additional information | - |
additional information | steady-state kinetic analysis, overview | Pyrococcus horikoshii | |
| 1.4.1.13 | 0.042 | - |
NADPH | pH 7.5, 37°C, pGLTY2 | Pyrococcus horikoshii |  |
| 1.4.1.13 | 0.11 | - |
NADPH | pH 7.5, 70°C, pGLTY2 | Pyrococcus horikoshii | |
| 1.4.1.13 | 6.42 | - |
NADPH | pH 7.5, 37°C, pGLTZ | Pyrococcus horikoshii | |
| 1.4.1.13 | 16.3 | - |
NADPH | pH 7.5, 70°C, pGLTZ | Pyrococcus horikoshii | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.4.1.13 | 51900 | - |
x * 51900, pGLTY2, SDS-PAGE, x * 52000, pGLTY1, SDS-PAGE | Pyrococcus horikoshii |
| 1.4.1.13 | 52000 | - |
x * 51900, pGLTY2, SDS-PAGE, x * 52000, pGLTY1, SDS-PAGE | Pyrococcus horikoshii |
| 1.4.1.13 | 52400 | - |
x * 52400, SDS-PAGE | Pyrococcus horikoshii |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.4.1.13 | L-glutamate + NADP+ + H2O | Pyrococcus horikoshii | - |
NH3 + 2-oxoglutarate + NADPH + H+ | - |
? | |
| 1.4.1.13 | NH3 + 2-oxoglutarate + NADPH + H+ | Pyrococcus horikoshii | - |
L-glutamate + NADP+ + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.4.1.13 | Pyrococcus horikoshii | A0A171 | orf PH0876 | - |
| 1.4.1.13 | Pyrococcus horikoshii | B3FYT6 | orf PH1873 | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.4.1.13 | L-glutamate + NADP+ + H2O | - |
Pyrococcus horikoshii | NH3 + 2-oxoglutarate + NADPH + H+ | - |
? | |
| 1.4.1.13 | additional information | assay with artificial eelectron acceptor iodonitrotetrazolium chloride | Pyrococcus horikoshii | ? | - |
? | |
| 1.4.1.13 | NH3 + 2-oxoglutarate + NADPH + H+ | - |
Pyrococcus horikoshii | L-glutamate + NADP+ + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.4.1.13 | ? | x * 51900, pGLTY2, SDS-PAGE, x * 52000, pGLTY1, SDS-PAGE | Pyrococcus horikoshii |
| 1.4.1.13 | ? | x * 52400, SDS-PAGE | Pyrococcus horikoshii |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.4.1.13 | GOGAT | - |
Pyrococcus horikoshii |
| 1.4.1.13 | pGLTY1 | - |
Pyrococcus horikoshii |
| 1.4.1.13 | pGLTY2 | - |
Pyrococcus horikoshii |
| 1.4.1.13 | pGLTZ | - |
Pyrococcus horikoshii |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.4.1.13 | 37 | - |
assay at | Pyrococcus horikoshii |
| 1.4.1.13 | 70 | - |
- |
Pyrococcus horikoshii |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.4.1.13 | 37 | 70 | - |
Pyrococcus horikoshii |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.4.1.13 | 70 | 100 | purified enzyme, 10 min, stable up to 90°C | Pyrococcus horikoshii |
| 1.4.1.13 | 100 | - |
purified enzyme, 10 min, loss of activity | Pyrococcus horikoshii |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.4.1.13 | 2.28 | - |
NADPH | pH 7.5, 37°C, pGLTY2 | Pyrococcus horikoshii | |
| 1.4.1.13 | 6.42 | - |
NADPH | pH 7.5, 37°C, pGLTZ | Pyrococcus horikoshii | |
| 1.4.1.13 | 16.3 | - |
NADPH | pH 7.5, 70°C, pGLTZ | Pyrococcus horikoshii | |
| 1.4.1.13 | 26.8 | - |
NADPH | pH 7.5, 70°C, pGLTY2 | Pyrococcus horikoshii | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.4.1.13 | 7.5 | - |
assay at | Pyrococcus horikoshii |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.4.1.13 | NADP+ | - |
Pyrococcus horikoshii | |
| 1.4.1.13 | NADPH | - |
Pyrococcus horikoshii | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.4.1.13 | evolution | phylogenetic and molecular evolutionary analyses | Pyrococcus horikoshii |
| 1.4.1.13 | physiological function | key enzyme in the early stages of ammonia assimilation in bacteria, algae and plants, catalyzing the reductive transamidation of the amido nitrogen from glutamine to 2-oxoglutarate to form two molecules of glutamate | Pyrococcus horikoshii |
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