Litcius/Paper detail

Bypassing the requirement for aminoacyl-tRNA by a cyclodipeptide synthase enzyme

Christopher J. Harding, Emmajay Sutherland, Jane G. Hanna, Douglas R. Houston, Clarissa Melo Czekster

2021RSC Chemical Biology13 citationsDOIOpen Access PDF

Abstract

enzyme, BtCDPS, which synthesises cyclo(l-Leu-l-Leu). We systematically tested where specificity arises and, in the process, uncovered small molecules (activated amino esters) that will suffice as substrates, although catalytically poor. We solved the structure of BtCDPS to 1.7 Å and combining crystallography, enzymatic assays and substrate docking experiments propose a model for how the minimal substrates interact with the enzyme. This work is the first report of a CDPS enzyme utilizing a molecule other than aa-tRNA as a substrate; providing insights into substrate requirements and setting the stage for the design of improved simpler substrates.

Topics & Concepts

Aminoacyl tRNA synthetaseEnzymeTransfer RNAATP synthaseChemistryBiochemistryAminoacyl-tRNARNAGeneRNA and protein synthesis mechanismsPeptidase Inhibition and AnalysisBiochemical and Molecular Research