Binding of substrate ligands to human blood group A and B glycosyltransferases causes long‐range perturbations in Ile side chains, reflecting the allosterically regulated binding mechanism. Chemical shift perturbations upon ligand binding massively exceed expected perturbations for active‐site amino acids, indicating high conformational plasticity of the enzymes.

中文翻译：

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底物与人血A和B组糖基转移酶结合的蛋白质NMR研究

底物配体与人类血液A和B组糖基转移酶的结合会引起Ile侧链的长期扰动，反映了变构调控的结合机制。配体结合后的化学位移扰动大大超过了活性位点氨基酸的预期扰动，表明酶的构象可塑性高。