Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | F4JKB6 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pre-tRNA-Gly precursor + H2O | analysis of the kinetics and cleavage-site selection by PRORP3 using precursor tRNAs (pre-tRNAs) with individual modifications at the canonical cleavage site, with either Rp- or Sp-phosphorothioate, or 2'-deoxy, 2'-fluoro, 2'-amino, or 2'-O-methyl substitutions. A small but robust rescue effect of Sp-phosphorothioate-modified pre-tRNA is observed in the presence of thiophilic Cd2+ ions,-consistent with metal-ion coordination to the (pro-)Sp-oxygen during catalysis. Sp-phosphorothioate, 2'-deoxy, 2'-amino, and 2'-O-methyl modification redirected the cleavage mainly to the next unmodified phosphodiester in the 5'-direction. The 2'-OH substituent at nucleotide -1 is involved in an H-bonding acceptor function. In contrast to bacterial RNase P, AtPRORP3 is able to utilize the canonical and upstream cleavage site with similar efficiency (corresponding to reduced cleavage fidelity), and the two cleavage pathways appear less interdependent than in the bacterial RNAbased system | Arabidopsis thaliana | tRNA-Gly + 5'-oligoribonucleotide | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PRORP3 | - |
Arabidopsis thaliana |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Arabidopsis thaliana |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Arabidopsis thaliana |