By Bernard L. Horecker, Earl R. Stadtman
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Additional info for Current topics in cellular regulation. Vol.13 : 1978
Chem. 2 5 0 , 6355-6361 (1975). 5. , Feliu, J. , Eur. J. Biochem. 3 7 , 1 4 8 - 1 5 6 (1973). 6. Cardenas, J. , and Dyson, R. , J. Biol. Chem. 2 4 8 , 6 9 3 8 - 6 9 4 4 (1973). 7. , Recondo, E . , and Rozengurt, E . , J. Biol. Chem. 2 4 3 , 3 0 5 1 - 3 0 5 6 (1968). 8. Clark, M . , Biochem. Biophys. Res. Commun. 6 8 , 120-126 (1976). 9. , Watson, D . C , and Dixon, G. , Eur. J. Biochem. 5 1 , 7 9 - 9 2 (1975). 10. Cori, G. , and Cori, C. , J. Biol. Chem. 1 5 8 , 3 2 1 - 3 3 2 (1945). 11. , Bade, E.
Maximally, 1 mole of phosphorus per mole of subunit can be bound to a specific serine residue in each subunit. It is clearly of interest to compare the kinetic properties of the phosphory lated enzyme with those of the unphosphorylated enzyme. In the studies so far reported maximally phosphorylated enzyme preparations have been used. 5 (20,45). 6 in the case of the pig and rat liver enzymes, respectively. At a saturat ing PEP concentration (5 mM) V m ax is the same for both enzyme forms (Fig.
This means that the Km of the heptapeptide approaches the concentration of pyruvate kinase subunits in rat liver (21,46,57). 01 mM the native enzyme is phosphorylated at about the same rate as the active pentapeptide but at a lower rate than the hexaand heptapeptides. In summary, the minimal structural requirements for a significant rate of phosphorylation of rat liver pyruvate kinase are fulfilled by the pentapeptide Arg-Arg-Ala-Ser-Val. Extension of the peptide by one or two amino acid residues makes it a better substrate for protein kinase, especially by increasing the affinity of the enzyme for the peptide.
Current topics in cellular regulation. Vol.13 : 1978 by Bernard L. Horecker, Earl R. Stadtman