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- W2092374178 abstract "Purified glycogen phosphorylase (α-1, 4-glucan:orthophosphate glucosyl transferase, E.C.2.4.1.1.) from Neurospora crassa shows a specific activity of 51 units/mg protein when measured in the direction of phosphorolysis by a new radiochemical assay. This compares to 148 units/mg protein when assayed in the direction of glycogen synthesis. The optimum pH of the enzyme is 6.5–8.0. Fluoride and pCMB are inhibitory. Glycogen, dextrin, and amylopectin are equally good substrates in the direction of phosphorolysis. In the synthesis direction glycogen was a superior primer. The enzyme follows normal Michaelis-Menten kinetics with respect to phosphate and glycogen. The Km values for phosphate and glycogen are 2.6–3.1 × 10−2m and 4.0 mg/ml respectively. Each Km value was independent of the concentration of the second substrate. AMP at 1.5 × 10−4m increased the Vmax 30% but had no effect on the Km values. Glucose-6-phosphate (Ki = 2.5–5.0 × 10−3 m) and UDPG (Ki = 4.4–5.5 × 10−3 m) are competitive inhibitors with respect to phosphate, as are ADPG and TDPG. UDPG and glucose-6-phosphate are both noncompetitive inhibitors with respect to glycogen. The inhibition of phosphorylase by UDPG and glucose-6-phosphate may play an important regulatory role in vivo. Arsenate was competitive with phosphate and noncompetitive with glycogen (Ki = 4–9 × 10−3 m). The enzyme was stabilized by glycogen and phosphate (but not by glucose-1-phosphate) against denaturation at 30 °. Rabbit muscle phosphorylase α phosphatase failed to convert the enzyme into an AMP-dependent form." @default.
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- W2092374178 date "1969-01-01" @default.
- W2092374178 modified "2023-10-14" @default.
- W2092374178 title "Neurospora crassa glycogen phosphorylase: Characterization and kinetics via a new radiochemical assay for phosphorolysis" @default.
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- W2092374178 doi "https://doi.org/10.1016/0003-9861(69)90547-5" @default.
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