L126G |
site-directed mutagenesis of a residue of the glutaminase subunit TrpG from anthranilate synthase, the mutant constitutively hydrolyzes glutamine in the absence of TrpE in contrast to the wild-type enzyme |
Thermotoga maritima |
L126G/V127Y/T129Y/Y131V |
site-directed mutagenesis of anthranilate synthase glutaminase subunit TrpG residues, the mutant constitutively hydrolyzes glutamine in the absence of TrpE in contrast to the wild-type enzyme |
Thermotoga maritima |
additional information |
in contrast to wild-type TrpG, two TrpG variants with single exchanges constitutively hydrolyze glutamine in the absence of TrpE. The introduced amino acid exchanges result in a distance reduction between the active site Cys-His pair, which facilitates the deprotonation of the sulfhydryl group of the catalytic cysteine and thus enables its nucleophilic attack onto the carboxamide group of the glutamine side chain, molecular dynamics simulations, overview |
Thermotoga maritima |
T129A |
site-directed mutagenesis of a residue of the glutaminase subunit TrpG from anthranilate synthase, the mutant shows no activity with glutamine in absence of TrpE like the wild-type enzyme |
Thermotoga maritima |
T129F |
site-directed mutagenesis of a residue of the glutaminase subunit TrpG from anthranilate synthase, the mutant constitutively hydrolyzes glutamine in the absence of TrpE in contrast to the wild-type enzyme |
Thermotoga maritima |
T129Y |
site-directed mutagenesis of a residue of the glutaminase subunit TrpG from anthranilate synthase, the mutant constitutively hydrolyzes glutamine in the absence of TrpE in contrast to the wild-type enzyme |
Thermotoga maritima |
V127Y |
site-directed mutagenesis of a residue of the glutaminase subunit TrpG from anthranilate synthase, the mutant shows no activity with glutamine in absence of TrpE like the wild-type enzyme |
Thermotoga maritima |
Y131V |
site-directed mutagenesis of a residue of the glutaminase subunit TrpG from anthranilate synthase, the mutant shows no activity with glutamine in absence of TrpE like the wild-type enzyme |
Thermotoga maritima |