Literature summary extracted from
Tatehashi, Y.; Takagi, H.
Characterization of gamma-glutamyl kinase mutants from Saccharomyces cerevisiae (2013), J. Biosci. Bioeng., 116, 576-579.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.7.2.11 |
gene PRO1 |
Saccharomyces cerevisiae |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.7.2.11 |
D154N |
site-directed mutagenesis, the mutant enzyme is less sensitive to proline feedback inhibition compared to the wild-type enzyme and shows an increased thermostability |
Saccharomyces cerevisiae |
2.7.2.11 |
I150T |
site-directed mutagenesis, the mutant enzyme is less sensitive to proline feedback inhibition compared to the wild-type enzyme and shows an increased thermostability |
Saccharomyces cerevisiae |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
2.7.2.11 |
L-proline |
feedback inhibition |
Saccharomyces cerevisiae |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.7.2.11 |
ATP + L-glutamate |
Saccharomyces cerevisiae |
- |
ADP + L-glutamate 5-phosphate |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.2.11 |
Saccharomyces cerevisiae |
P32264 |
gene PRO1 |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.7.2.11 |
ATP + L-glutamate |
- |
Saccharomyces cerevisiae |
ADP + L-glutamate 5-phosphate |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.7.2.11 |
More |
enzyme domain organization, overview |
Saccharomyces cerevisiae |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.2.11 |
gamma-glutamyl kinase |
- |
Saccharomyces cerevisiae |
2.7.2.11 |
scGK |
- |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
2.7.2.11 |
30 |
- |
assay at |
Saccharomyces cerevisiae |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
2.7.2.11 |
7.4 |
- |
assay at |
Saccharomyces cerevisiae |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
2.7.2.11 |
ATP |
- |
Saccharomyces cerevisiae |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.7.2.11 |
malfunction |
Yeast cells expressing mutant enzymes D154N and I150T accumulate proline and show a higher tolerance to various stresses, including freezing, ethanol, osmotic pressure, and heat shock |
Saccharomyces cerevisiae |
2.7.2.11 |
metabolism |
gamma-glutamyl kinase is a key enzyme in the Saccharomyces cerevisiae proline biosynthesis pathway |
Saccharomyces cerevisiae |
2.7.2.11 |
additional information |
residues Asp154 and Ile150 in the Saccharomyces cerevisiae gamma-glutamate kinase are important for allosteric regulation and the affinity with L-proline and L-glutamate, but not with ATP. The PUA domain itself is required for the full display of enzyme activity, but is not involved in the allosteric regulation and the affinity with substrates and proline. The proline-auxotrophic yeast strain BY4741DELTApro1DELTAcar2 that expresses the PUA domain deletion-mutant grows even on proline-free medium, although a growth defect is observed |
Saccharomyces cerevisiae |