Matches in DBpedia 2016-04 for { ?s ?p "RNase PH is a 3'-5' exoribonuclease and nucleotidyltransferase, present in archaea and bacteria, that is involved in tRNA processing. Contrary to hydrolytic enzymes, it is a phosphorolytic enzyme, meaning that it uses inorganic phosphate as a reactant to cleave nucleotide-nucleotide bonds, releasing diphosphate nucleotides. The active structure of the proteins is actually a homohexameric complex, consisting of three ribonuclease (RNase) PH dimers."@en }
Showing triples 1 to 2 of
2
with 100 triples per page.
- RNase_PH comment "RNase PH is a 3'-5' exoribonuclease and nucleotidyltransferase, present in archaea and bacteria, that is involved in tRNA processing. Contrary to hydrolytic enzymes, it is a phosphorolytic enzyme, meaning that it uses inorganic phosphate as a reactant to cleave nucleotide-nucleotide bonds, releasing diphosphate nucleotides. The active structure of the proteins is actually a homohexameric complex, consisting of three ribonuclease (RNase) PH dimers.".
- Q3415271 comment "RNase PH is a 3'-5' exoribonuclease and nucleotidyltransferase, present in archaea and bacteria, that is involved in tRNA processing. Contrary to hydrolytic enzymes, it is a phosphorolytic enzyme, meaning that it uses inorganic phosphate as a reactant to cleave nucleotide-nucleotide bonds, releasing diphosphate nucleotides. The active structure of the proteins is actually a homohexameric complex, consisting of three ribonuclease (RNase) PH dimers.".