PMID: 2105076Jan 1, 1990Paper

Kinetic analysis of the separate phosphorylation events in the phosphorylase kinase reaction

Archives of Biochemistry and Biophysics
W R Harris, D J Graves

Abstract

Glycogen phosphorylase, a dimer of identical subunits, is activated by phosphorylase kinase-catalyzed phosphorylation of one serine residue in each subunit. In this paper, the effect of the phosphorylation of one subunit on the phosphorylation of the other subunit was examined. The three forms of phosphorylase, phosphorylase b (nonphosphorylated), phosphorylase ab (one subunit phosphorylated), and phosphorylase a (both subunits phosphorylated), were separated by anion-exchange high-performance liquid chromatography (HPLC). Purified phosphorylase ab was found to be stable under the conditions of the phosphorylase kinase assay. Initial rate kinetics showed that phosphorylase kinase had a lower KM for phosphorylase ab (3.9 +/- 0.24 microM) than for phosphorylase b (14.9 +/- 2.6 microM). Using the HPLC separation as a simultaneous assay for the three forms of phosphorylase during the phosphorylase kinase reaction, it was found that the pseudo-first-order rate constant for the second phosphorylation step (k2) was 3.7 times greater than that for the first step (k1). The activator AMP reduced the ratio k2/k1 from 3.7 without AMP to 1.4. When the monomeric gamma delta complex of phosphorylase kinase subunits was used as the enzyme, the...Continue Reading

References

Nov 5, 1979·Journal of Molecular Biology·L N JohnsonI T Weber
Nov 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·K TitaniE H Fischer
Dec 21, 1972·Doklady Akademii nauk SSSR·N B LivanovaG V Silonova
Jan 4, 1973·Biochemical and Biophysical Research Communications·G Tessmer, D J Graves
Jul 2, 1973·Biochemical and Biophysical Research Communications·J I Tu, D J Graves
Jul 1, 1980·Analytical Biochemistry·R Marusyk, A Sergeant
Jan 4, 1965·Biochemical and Biophysical Research Communications·J H WANGD J GRAVES

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Citations

Oct 1, 1994·Protein Science : a Publication of the Protein Society·L N Johnson, D Barford

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