Preparation and properties of highly-purified Vibrio costicola polynucleotide phosphorylase.
Vibrio costicola polynucleotide phosphorylase (polyribonucleotide: orthophosphate nucleotidyltransferase, EC 2.7.7.8) has been purified to electrophoretic homogeneity. It has an approximate molecular weight of 220 000 and consists of identical subunits with an approximate molecular weight of 72 000. The enzyme appears to be a fairly typical polynucleotide phosphorylase with respect to its pH optima, substrate specificity and requirement for a divalent cation cofactor. However, the effect of salt concentration on its physiologically important phosphorolysis activity suggests that it is a moderately halophilic enzyme, able to function at the intracellular ionic strength of the bacterium. In addition, its ADP polymerization activity is remarkably stimulated by polylysine.
D000244:Adenosine Diphosphate / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D008970:Molecular Weight; D011061:Poly A / Q000494:pharmacology; D011107:Polylysine / Q000494:pharmacology; D011108:Polymers / Q000378:metabolism; D011117:Polyribonucleotide Nucleotidyltransferase / Q000378:metabolism*; D011189:Potassium Chloride / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology; D014733:Vibrio / Q000201:enzymology*
D011108:Polymers; D011061:Poly A; D011107:Polylysine; D008345:Manganese; D012965:Sodium Chloride; D000244:Adenosine Diphosphate; D011189:Potassium Chloride; D011117:Polyribonucleotide Nucleotidyltransferase; D008274:Magnesium