2023
DOI: 10.1093/nar/gkad205
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Design principles and functional basis of enantioselectivity of alanyl-tRNA synthetase and a chiral proofreader during protein biosynthesis

Abstract: Homochirality of the cellular proteome is attributed to the L-chiral bias of the translation apparatus. The chiral specificity of enzymes was elegantly explained using the ‘four-location’ model by Koshland two decades ago. In accordance with the model, it was envisaged and noted that some aminoacyl-tRNA synthetases (aaRS) that charge larger amino acids are porous to D-amino acids. However, a recent study showed that alanyl-tRNA synthetase (AlaRS) can mischarge D-alanine and that its editing domain, but not the… Show more

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“…The stereoisomeric recognition of biomolecules in nature exhibits a noteworthy level of specificity, resulting in two mirror image permutations of enantiomers that elicit quite different biological reactions. , In this context, chiral amino acids play a crucial role in various metabolic processes and serve as indispensable building blocks for proteins and other biomolecules. , In recent years, there has been a shift in emphasis from proteogenic l -amino acids to the emerging biological significance of several d -antipodes. Free d -amino acids have been unveiled to play crucial biological and pathological roles in living organisms. Although many specific physiological functions are still being investigated, d -amino acids have garnered increasing attention as potential disease markers and for the treatment of neurological disorders, such as schizophrenia, Parkinsonism syndrome, and Alzheimer’s disease. Additionally, the structural diversity of naturally occurring amino acids has found extensive applications in the chemical industry , and pharmaceutical sciences. Two types of enantiomers have become inestimable initial ingredient for the stereoselective synthesis of physiological activators and novel functional materials . Consequently, the exploitation of sensitive and accessible analytical techniques to discriminate between enantiomers of amino acids is extraordinarily attractive and challenging.…”
Section: Introductionmentioning
confidence: 99%
“…The stereoisomeric recognition of biomolecules in nature exhibits a noteworthy level of specificity, resulting in two mirror image permutations of enantiomers that elicit quite different biological reactions. , In this context, chiral amino acids play a crucial role in various metabolic processes and serve as indispensable building blocks for proteins and other biomolecules. , In recent years, there has been a shift in emphasis from proteogenic l -amino acids to the emerging biological significance of several d -antipodes. Free d -amino acids have been unveiled to play crucial biological and pathological roles in living organisms. Although many specific physiological functions are still being investigated, d -amino acids have garnered increasing attention as potential disease markers and for the treatment of neurological disorders, such as schizophrenia, Parkinsonism syndrome, and Alzheimer’s disease. Additionally, the structural diversity of naturally occurring amino acids has found extensive applications in the chemical industry , and pharmaceutical sciences. Two types of enantiomers have become inestimable initial ingredient for the stereoselective synthesis of physiological activators and novel functional materials . Consequently, the exploitation of sensitive and accessible analytical techniques to discriminate between enantiomers of amino acids is extraordinarily attractive and challenging.…”
Section: Introductionmentioning
confidence: 99%