leuS Antibody

1. Zinc is the molecular "switch" that controls the catalytic cycle of bacterial leucyl-tRNA synthetase PMID: 25450019
2. The prime biological function of LeuRS editing is to prevent mis-incorporation of the non-standard amino acid norvaline. PMID: 24935946
3. This work provides an assessment of how intra-molecular translocation of the tRNA CCA-tail balances the aminoacylation and editing activities of LeuRS. PMID: 23585282
4. threonine residues (Thr(252)), (Thr(247), and Thr(248)) play a central role in amino acid editing PMID: 16300391
5. Conserved arginine & threonine at respective sites in LeuRS & IleRS diverged to confer amino acid substrate recognition. This site complements other sites in amino acid binding pocket of editing active site of E coli LeuRS, including Thr252 & Val338. PMID: 17311409
6. beta-strands, which link the CP1 domain to the aminoacylation core of LeuRS, are required for editing of mischarged tRNALeu PMID: 17474713
7. Multiple nonstandard as well as standard amino acids were toxic to the cell when LeuRS editing was inactivated PMID: 17890314
8. identified specific residues within the beta-strand tethers that selectively impact enzyme activity, supporting the idea that beta-strand orientation is crucial for Leucyl-tRNA synthetase canonical core and CP1 domain functions PMID: 18363380
9. A point mutation in CP1 of class I leucyl-tRNA synthetase inactivates deacylase activity and produces misacylated tRNA, although deletion of the entire CP1 domain also disabled the deacylase activity PMID: 19020078

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KEGG: ecj:JW0637

STRING: 316385.ECDH10B_0711