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- W1966961505 abstract "Hypoxanthine phosphoribosyltransferase (EC 2.4.2.8) of a strain of Streptomyces cyanogenus was purified 1, 900-fold to an apparent homogenity from cell-free extracts. The enzyme had a molecular weight of 150, 000 and consisted of eight identical subunits with a molecular weight of 18, 000. The isoelectric point was at pH 4.4. The enzyme required Mg2+ or Mn2+ for activity and had a pH optimum at 8.5. Hypoxanthine and guanine were good substrates for the enzyme. Xanthine was a very poor substrate and adenine was not a substrate. Apparent Km values of the enzyme for hypoxanthine, guanine and 5-phosphoribose-l-pyro-phosphate were 1.6×10-6, 2.7×10-6 and 6.3×10-5 at, respectively. All purine nucleotides tested inhibited the activity significantly, apparently by competing with 5-phosphoribose-l-pyrophosphate." @default.
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- W1966961505 date "1980-01-01" @default.
- W1966961505 modified "2023-09-26" @default.
- W1966961505 title "Studies on the control of purine base metabolism in Streptomyces. Part V. Purification and properties of hypoxanthine phosphoribosyltransferase from Streptomyces cyanogenus." @default.
- W1966961505 doi "https://doi.org/10.1271/bbb1961.44.1999" @default.
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