Báo cáo khoa học: Tyr235 of human cytosolic phosphoenolpyruvate carboxykinase influences catalysis through an anion–quadrupole interaction with phosphoenolpyruvate carboxylate
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Tyr235 of GTP-dependent phosphoenolpyruvate (PEP) carboxykinase is afully invariant residue. The aromatic ring of this residue establishes anenergetically favorable weak anion–quadrupole interaction with PEPcarboxylate. The role of Tyr235 in catalysis was investigated via kineticanalysis of site-directed mutagenesis-derived variants.
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Tyr235 of human cytosolic phosphoenolpyruvate carboxykinase influences catalysis through an anion–quadrupole interaction with phosphoenolpyruvate carboxylate
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Tyr235 of human cytosolic phosphoenolpyruvate carboxykinase influences catalysis through an anion–quadrupole interaction with phosphoenolpyruvate carboxylate
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