EC Number |
General Information |
Reference |
---|
4.6.1.18 | evolution |
the enzyme belongs to the pancreatic-type secretory ribonuclease superfamily |
729310 |
4.6.1.18 | evolution |
the enzyme belongs to the pancreatic-type secretory ribonuclease superfamily as a unique natively dimeric member |
729310 |
4.6.1.18 | evolution |
the enzyme belongs to the vertebrate pancreatic-like RNase A superfamily, sequence comparisons and phylogenetic analysis, overview |
729713 |
4.6.1.18 | evolution |
the enzyme is a member of the pancreatic ribonuclease (RNase) superfamily |
730422 |
4.6.1.18 | evolution |
the enzyme is one of the key models in studies of evolutionary innovation and functional diversification, evolution and the function of Caniformia RNASE1 genes, phylogenetic analysis, overview. Four independent gene duplication events in the families of superfamily Musteloidea, including Procyonidae, Ailuridae, Mephitidae and Mustelidae |
730952 |
4.6.1.18 | malfunction |
mechanistic model for the denaturation of bovine pancreatic ribonuclease A in urea, a direct interaction between urea and protonated histidine as the initial step for protein inactivation followed by hydrogen bond formation with polar residues, and the breaking of hydrophobic collapse as the final steps for protein denaturation |
707508 |
4.6.1.18 | malfunction |
RNase A tandem enzymes, in which two RNase A molecules are artificially connected by a peptide linker, and thus have a pseudodimeric structure, exhibit remarkable cytotoxic activity, but can be inhibited by the cytosolic ribonuclease inhibitor in vitro. Structure modeling, overview |
717596 |
4.6.1.18 | metabolism |
the enzyme lacks cytotoxic activity as it is inactivated by intracellular cytosolic ribonuclease inhibitor |
750772 |
4.6.1.18 | more |
analysis of synthesis and maturation, folding, quality control, and secretion, of pancreatic RNase in the endoplasmic reticulum of live cells, overview. Human RNase folds rapidly and is secreted mainly in glycosylated forms |
717861 |
4.6.1.18 | more |
analysis of synthesis and maturation, folding, quality control, and secretion, of pancreatic RNase in the endoplasmic reticulum of live cells, overview. In contrast to the slow in vitro refolding, the protein folds almost instantly after translation and translocation into the endoplasmatic reticulum lumen. Despite high stability of the native protein, only about half of the RNase reaches a secretion competent, monomeric form and is rapidly transported from the rough endoplasmic reticulum via the Golgi complex to the extracellular space |
717861 |