Nucleoside phosphorylase activity of Octopus vulgaris hepatopancreas.
From a research on partially purified extracts of Octopus vulgaris hepatopancreas a number of properties of the nucleosidase present in such extracts have been defined, such as enzyme affinity towards different purine and pyrimidine ribo- and deoxyribo-nucleosides. The phosphorolytic mechanism of action of the Octopus enzyme system is similar to the mechanism already known for many nucleosidases from animal tissues. The possibility is envisaged of two different nucleosidases being present, one specific for ribonucleosides, with an acid optimum pH, and the other one for deoxyribonucleosides, with an alkaline pH optimum. Adenosine deaminase also appears to be a component of Octopus hepatopancreas.
D000818:Animals; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology; D049831:Octopodiformes / Q000201:enzymology*; D010179:Pancreas / Q000201:enzymology; D010430:Pentosyltransferases / Q000378:metabolism*; D011684:Purine Nucleosides; D011683:Purine-Nucleoside Phosphorylase / Q000378:metabolism*; D011741:Pyrimidine Nucleosides; D013379:Substrate Specificity
D011684:Purine Nucleosides; D011741:Pyrimidine Nucleosides; D010430:Pentosyltransferases; D011683:Purine-Nucleoside Phosphorylase