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Literature summary extracted from

  • Tatehashi, Y.; Takagi, H.
    Characterization of gamma-glutamyl kinase mutants from Saccharomyces cerevisiae (2013), J. Biosci. Bioeng., 116, 576-579.
    View publication on PubMed

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