EC Number |
Protein Variants |
Reference |
---|
6.3.5.2 | GP-1 |
psicofuranine, decoyinine and adenosine strongly inhibit wild type enzyme. Mutant enzyme GP-1 shows decreased inhibition with adenosine and psicofuranine, but inhibition by decoyinine does not vary, complete loss of inhibition in mutant MG-1 |
1379 |
6.3.5.2 | more |
construction of disruption mutants, the heterozygote GUA1/gua1 strain is hypersensitive to 6-azauracil, a known inhibitor of the IMP dehydrogenase involved in GMP biosynthesis. In a murine model of systemic candidiasis, the virulence of the heterozygous strain is marginally attenuated, while the homozygous mutant gua1/gua1 strain is completely avirulent |
-, 703766 |
6.3.5.2 | C95A |
mutant defective in glutamine hydrolysis. The phenotype of ectopic coexpression of USP7 witheither S242L or C95A is similar to that resulting from the coexpression of WT GMPS. Ectopic overexpression of only mutation S242L, mutation C95A, or USP7 mutation C250A has no effect on eye development |
705708 |
6.3.5.2 | S242L |
mutant defective in ATP hydrolysis. The phenotype of ectopic coexpression of USP7 with either S242L or C95A is similar to that resulting from the coexpression of WT GMPS. Ectopic overexpression of only mutation S242L, mutation C95A, or USP7 mutation C250A has no effect on eye development |
705708 |
6.3.5.2 | C102A |
totally devoid of glutamine-dependent activity. Kinetic constants for NH4Cl, ATP, and XMP obtained for the ammonia-dependent activity are similar to that of the wild-type enzyme |
714242 |
6.3.5.2 | G388D |
reduces the activity of GMP synthase Gua1 in budding yeast and the total G-nucleotide pool, leading to precipitous reductions in the GDP/GTP ratio and ATP level in vivo. G388D strongly reduces the rate of growth, impairs general protein synthesis, and derepresses translation of GCN4 mRNA, encoding a transcriptional activator of diverse amino acid biosynthetic enzymes. Although processing of pre-tRNAi Met and other tRNA precursors, and the aminoacylation of tRNAi Met are also strongly impaired in G388D cells, tRNAi Met-containing complexes with the macromolecular composition of the eIF2tRNAi Met.GTP complex and the multifactor complex required for translation initiation accumulate 10-fold in G388D cells and, to a lesser extent, in wild-type cells treated with 6-azauracil |
715121 |
6.3.5.2 | 37W |
the mutant shows severely reduced specific activity compared to the wild type enzyme |
727023 |
6.3.5.2 | W37A |
the mutant shows slightly reduced specific activity compared to the wild type enzyme |
727023 |
6.3.5.2 | E383A |
8fold decrease in glutaminase activity |
744157 |
6.3.5.2 | H186A |
30-50 fold decrease in Km value for glutamine |
744157 |