EC Number   |
Protein Variants |
Reference |
|---|
    6.1.1.5 | AIleRS |
mutant enzymes IleRS(C922S) and AIleRS with replacement of Cys922 through Ala939 with a 33 amino acid peptide unable to bind zinc. Mutant enzymes have altered zinc binding and aminoacylation activity |
450 |
| 6.1.1.5 | D333A |
site-directed mutagenesis, solution-based Val-AMP hydrolysis is 25fold slower than the rate of AMP formation assigned to editing in mutant D333A ScIleRS, non-enzymatic hydrolysis only weakly contributes to AMP accumulation |
-, 745362 |
| 6.1.1.5 | D334A |
site-directed mutagenesis, the post-transfer editing-defective mutant of SgIleRS displays the similar rates of aminoacylation and AMP formation in the presence of valine, exhibiting a kAMP/kVal-tRNA ratio of 1.1. Stoichiometric ATP consumption in Val-tRNAIle synthesis demonstrates the lack of proofreading by D334A SgIleRS, arguing against hydrolysis of Val-AMP alongside aminoacylation within the synthetic site, SgIleRS naturally lacks tRNA-dependent pre-transfer editing |
745362 |
| 6.1.1.5 | D342A |
site-directed mutagenesis, the IleRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations |
715519 |
| 6.1.1.5 | D342A |
site-directed mutagenesis, the mutant exhibits slightly reduced aminoacylation activity compared to the wild-type enzyme, the post-transfer editing deficient D342A IleRS accumulates AMP by pretransfer editing and by tRNA misacylation when the noncognate aa-AMP evades this hydrolytic reaction, neither wild-type nor D342A IleRS significantly deacylates Ile-tRNAIle under steady-state conditions |
744324 |
| 6.1.1.5 | D539A/W541A |
catalytically inactive |
727946 |
| 6.1.1.5 | E708K |
naturally occuring mutation found in a heterozygous patient, the mutation is at the junction of the catalytic core domain and the anticodon-binding domain, and is predicted to be disease-causing |
745057 |
| 6.1.1.5 | F227L |
the naturally occuring mutation affects the muciprocin binding |
675256 |
| 6.1.1.5 | G590D |
pseudomonic-acid resistant mutant MBT10, with a Gly590 to aspartic acid transition |
-, 459 |
| 6.1.1.5 | H319A |
site-directed mutagenesis, Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain, but the mutant shows detectable editing activities against the cognate isoleucine, mechanism, overview |
675388 |
