title: Expanding a tyrosyl-tRNA synthetase assay to other aminoacyl-tRNA synthetases.
abstract: Aminoacyl-tRNA synthetases catalyze the attachment of amino acids to their cognate tRNAs. In general, aminoacyl-tRNA synthetase assays require stoichiometric amounts of tRNA, which limits their sensitivity while increasing their cost. This requirement for stoichiometric amounts of tRNA can be alleviated if the aminoacyl-tRNA product is cleaved following the tRNA aminoacylation reaction, regenerating the free tRNA substrate. This data article is related to the research article entitled "A continuous tyrosyl-tRNA synthetase assay that regenerates the tRNA substrate" in which this approach is used to develop a continuous spectrophotometric assay for tyrosyl-tRNA synthetase [1]. Here we present enzymes that can be used to cleave the aminoacyl-tRNA product for at least 16 of the 20 naturally occurring amino acids. These enzymes can be used to extend the tyrosyl-tRNA synthetase assay to other aminoacyl-tRNA synthetases.
authors.affiliation: Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center in Shreveport, 1501 Kings Highway, Shreveport, LA 71130, USA.
authors.forename: Charles J
authors.initials: CJ
authors.lastname: Richardson
authors.affiliation: Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center in Shreveport, 1501 Kings Highway, Shreveport, LA 71130, USA.
authors.forename: Eric A
authors.initials: EA
authors.lastname: First
keywords: Aminoacyl-tRNA synthetase; Cyclodipeptide synthase; Editing domain; High-throughput assay; d-tyrosyl-tRNA deacylase