Glycogen-bound polyphosphate kinase from the archaebacterium Sulfolobus acidocaldarius.
Glycogen-bound polyphosphate kinase has been isolated from a crude extract of Sulfolobus acidocaldarius by isopycnic centrifugation in CsCl. Divalent cations (Mn2+ greater than Mg2+) stimulated the reaction. The enzyme does not require the presence of histones for its activity; it is inhibited strongly by phosphate and slightly by fluoride. The protein from the glycogen complex migrated in a sodium dodecyl sulfate-polyacrylamide gel as a 57-kilodalton protein band; after isoelectric focusing it separated into several spots in the pH range of 5.6 to 6.7.
Skórko
R
R
Lehrstuhl für Mikrobiologie, Universität Regensburg, Federal Republic of Germany.
Osipiuk
J
J
Stetter
K O
KO
D006003:Glycogen / Q000302:isolation & purification*; D006091:Gram-Negative Chemolithotrophic Bacteria / Q000201:enzymology*; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D008970:Molecular Weight; D010770:Phosphotransferases / Q000302:isolation & purification* / Q000378:metabolism; D017856:Phosphotransferases (Phosphate Group Acceptor); D011485:Protein Binding
D008345:Manganese; D006003:Glycogen; D010770:Phosphotransferases; D017856:Phosphotransferases (Phosphate Group Acceptor); C022424:polyphosphate kinase; D008274:Magnesium