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From the tryptic digests of phosphorylated snake muscle FruP_(2ase), a phosphoryl peptide has beenisolated, its amino acid sequence was Gly-Ala-Gly-Ser-Arg and the phosphorylation site was consideredto be on the serine residue. Effectors of the enzyme such as FruP_2, F6P and AMP did not affect thephosphorylation. The effect of pH on phosphorylation was consistent with that on the activity of theenzyme. The activity of phosphorylated enzyme was slightly lower than that of the native enzyme, thisdifference in activities between the two forms of the enzyme increased with decreasing the substrateconcentration. Results further support that a phosphorylated intermediate is involved in the catalytic reac-tion of FruP_(2ase).
From the tryptic digests of phosphorylated snake muscle FruP_ (2ase), a phosphoryl peptide has beenisolated, its amino acid sequence was Gly-Ala-Gly-Ser-Arg and the phosphorylation site was considered to be on the serine residue. Effectors of the enzyme such The effect of pH on phosphorylation was consistent with that on the activity of the enzyme. The activity of phosphorylated enzyme was slightly lower than that of the native enzyme, thisdifference in activities between the two forms of the enzyme increased with decreasing the substrate concentration. The more support that a phosphorylated intermediate is involved in the catalytic reactivation of FruP_ (2ase).