Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase

Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase Descriptor: 4-O-methyl-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranosyl fluoride, 4-O-methyl-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-2)-5-fluoro-alpha-L-idopyranose, CALCIUM ION, ... Authors: Li, C, Zhang, R, Withers, S.G, Brayer, G.D. Deposit date: 2009-08-03 Release date: 2009-10-27 Last modified: 2024-10-30 Method: X-RAY DIFFRACTION (2 Å) Cite: Directed "in situ" inhibitor elongation as a strategy to structurally characterize the covalent glycosyl-enzyme intermediate of human pancreatic alpha-amylase Biochemistry, 48, 2009

定向"原位"延伸策略：表征人胰腺α-淀粉酶（α-Amylase）的共价糖基-酶催化中间体
底物描述：4-O-甲基-α-D-吡喃葡萄糖-(1→4)-α-D-吡喃葡萄糖基氟化物、4-O-甲基-α-D-吡喃葡萄糖-(1→4)-β-D-吡喃葡萄糖-(1→2)-5-氟-α-L-艾杜吡喃糖、钙离子（CALCIUM ION）等。
作者：Li, C、Zhang, R、Withers, S.G.、Brayer, G.D.
提交日期：2009-08-03
发布日期：2009-10-27
最后修改日期：2024-10-30
实验方法：X射线衍射（2 Å）
引用：《定向"原位"抑制剂延伸策略：结构表征人胰腺α-淀粉酶的共价糖基-酶催化中间体》，刊载于《生物化学（Biochemistry）》第48卷，2009年