The eukaryotic tRNA-guanine transglycosylase enzyme inserts queuine into tRNAviaa sequential bi–bi mechanism
| Autor: | Vincent P. Kelly, Claire Fergus, Stephen J. Connon, J. Mike Southern, Mashael A. Alqasem |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Guanine
Cooperativity Wobble base pair Catalysis 03 medical and health sciences chemistry.chemical_compound RNA Transfer Materials Chemistry Pentosyltransferases 030304 developmental biology chemistry.chemical_classification 0303 health sciences 030302 biochemistry & molecular biology Metals and Alloys Substrate (chemistry) Queuine General Chemistry Surfaces Coatings and Films Electronic Optical and Magnetic Materials Amino acid Enzyme chemistry Biochemistry Transfer RNA Ceramics and Composites |
| Zdroj: | Chemical Communications. 56:3915-3918 |
| ISSN: | 1364-548X 1359-7345 |
| DOI: | 10.1039/c9cc09887a |
| Popis: | Eukaryotic tRNA-guanine transglycosylase (TGT) - an enzyme recently recognised to be of potential therapeutic importance - catalyses base-exchange of guanine for queuine at the wobble position of tRNAs associated with 4 amino acids via a distinct mechanism to that reported for its eubacterial homologue. The presence of queuine is unequivocally required as a trigger for reaction between the enzyme and tRNA and exhibits cooperativity not seen using guanine as a substrate. |
| Databáze: | OpenAIRE |
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