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Literature summary for 2.7.2.11 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
Search for more literature for 2.7.2.11

Cloned(Commentary)

Cloned (Comment) Organism
gene PRO1 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
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
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

Inhibitors Comment Organism Structure
L-proline feedback inhibition Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamate Saccharomyces cerevisiae
-
 ADP + L-glutamate 5-phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P32264 gene PRO1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamate
-
 Saccharomyces cerevisiae ADP + L-glutamate 5-phosphate
-
 ?

Subunits

Subunits Comment Organism
More enzyme domain organization, overview Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
gamma-glutamyl kinase
-
 Saccharomyces cerevisiae
scGK
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
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
metabolism gamma-glutamyl kinase is a key enzyme in the Saccharomyces cerevisiae proline biosynthesis pathway Saccharomyces cerevisiae
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