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Literature summary extracted from

  • Biterova, E.I.; Barycki, J.J.
    Structural basis for feedback and pharmacological inhibition of Saccharomyces cerevisiae glutamate cysteine ligase (2010), J. Biol. Chem., 285, 14459-14466.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.2.2 structure of the GCL-glutathione complex to 2.5 A resolution indicates that the inhibitor occupies both the glutamate- and the presumed cysteine-binding site and disrupts the previously observed Mg2+-coordination in the ATP-binding site. The structure of the complex with mechanism-based inhibitor L-buthionine-S-sulfoximine to 2.2 A resolution confirms that L-buthionine-S-sulfoximine is phosphorylated on the sulfoximine nitrogen to generate the inhibitory species and reveals contacts that likely contribute to transition state stabilization Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
6.3.2.2 C266A about 2fold increase in both Km and Ki value Saccharomyces cerevisiae
6.3.2.2 C266S about 2fold increase in both Km and Ki value Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.2.2 gamma-L-Glu-L-Cys
-
 Saccharomyces cerevisiae
6.3.2.2 glutathione feedback-regulation. The structure of the GCL-glutathione complex to 2.5 A resolution indicates that the inhibitor occupies both the glutamate- and the presumed cysteine-binding site and disrupts the previously observed Mg2+-coordination in the ATP-binding site Saccharomyces cerevisiae
6.3.2.2 L-buthionine-S-sulfoximine mechanism-based inhibitor. The crystal structure of the enzyme complex to 2.2 A resolution confirms that L-buthionine-S-sulfoximine is phosphorylated on the sulfoximine nitrogen to generate the inhibitory species and reveals contacts that likely contribute to transition state stabilization Saccharomyces cerevisiae
6.3.2.2 L-Glu
-
 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.2.2 0.08
-
 ATP wild-type, pH 8.0 Saccharomyces cerevisiae
6.3.2.2 0.17
-
 L-Cys wild-type, pH 8.0 Saccharomyces cerevisiae
6.3.2.2 1.21
-
 L-Glu wild-type, pH 8.0 Saccharomyces cerevisiae
6.3.2.2 1.93
-
 L-Glu mutant C266A, pH 8.0 Saccharomyces cerevisiae
6.3.2.2 2.15
-
 L-Glu mutant C266S, pH 8.0 Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.2 Saccharomyces cerevisiae P32477
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.2 ATP + L-Glu + L-Cys
-
 Saccharomyces cerevisiae ADP + phosphate + gamma-L-Glu-L-Cys
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.3.2.2 2.12
-
 gamma-L-Glu-L-Cys wild-type, pH 8.0 Saccharomyces cerevisiae
6.3.2.2 3.93
-
 L-Glu mutant C266S, pH 8.0 Saccharomyces cerevisiae
6.3.2.2 4.7
-
 L-Glu mutant C266A, pH 8.0 Saccharomyces cerevisiae