The taxonomic range for the selected organisms is: Saccharomyces cerevisiae The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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
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
an ubiquitine conjugated protein, induces gamma-glutamylcysteine synthetase expression only in glutathione synthetase-dficient mutants, not in the wild-type
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
structures of glutamate cysteine ligase in the presence of glutamate and MgCl2, to 2.1 A resolution, and in complex with glutamate, MgCl2, and ADP to 2.7 A resolution. Structures reveal an unusual binding pocket for the alpha-carboxylate of the glutamate substrate and an ATP-independent Mg2+ coordination site, clarifying the Mg2+-dependence of the enzymatic reaction
mutants with a deletion of GSH1 cannot grow, a high level expression from a plasmid of the enzyme can compensate for adeletion of gene GSH2 encoding glutathione synthatase, the enzyme catalyzing the second step of glutathione biosynthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, gene GSH1 maps to chromosome X, expression in and functional complementation of an enzyme-deficient mutant strain, the yAP-1 responsive element in the promotor of gene GSH1 is involved in transcription of the gene in response to exposure to cadmium or hydrogen peroxide
a recombinant plasmid, pGMF, containing a gamma-glutamylcysteine synthetase gene (GSH-I) from Saccharomyces cerevisiae, is constructed with a copper-resistance gene as the selection marker and introduced into Saccharomyces cerevisiae YSF-31. The glutathione content of the recombinant strain is 1.5fold (13.1 mg/g*dry cells) of that in the host strain
expression of the enzyme at high level in deletion mutant strains of GHS1 and GSH2, the latter encoding the glutathione synthetase, the GSH1 promotor is Met4-inducible and GSH repressible