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Article

Substrate specificity and catalysis by the editing active site of Alanyl-tRNA synthetase from Escherichia coli.

Biochemistry - 8 Mar 2011

Pasman Zvi, Robey-Bond Susan, Mirando Adam C, Smith Gregory J, Lague Astrid, Francklyn Christopher S

Abstract excerpt

Aminoacyl-tRNA synthetases (ARSs) enhance the fidelity of protein synthesis through multiple mechanisms, including hydrolysis of the adenylate and cleavage of misacylated tRNA. Alanyl-tRNA synthetase (AlaRS) limits misacylation with glycine and serine by use of a dedicated editing domain, and a mutation in this activity has been genetically linked to a mouse model of a progressive neurodegenerative disease. Using...

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Identifiers

PMID: 21241052
DOI: 10.1021/bi1013535
PMCID: PMC3069921

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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