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: (2R,3S,4R,5R,6R)-2,6-difluoro-2-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol, 5-fluoro-alpha-L-idopyranose, CALCIUM ION, ... Authors: Li, C, Zhang, R, Withers, S.G, Brayer, G.D. Deposit date: 2009-08-04 Release date: 2009-10-27 Last modified: 2024-11-06 Method: X-RAY DIFFRACTION (1.43 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’延伸策略用于表征人胰腺α-淀粉酶（α-amylase）的共价糖基-酶催化中间体
组分描述：(2R,3S,4R,5R,6R)-2,6-二氟-2-(羟甲基)四氢-2H-吡喃-3,4,5-三醇、5-氟-α-L-艾杜吡喃糖、钙离子（CALCIUM ION）……
作者：李（Li, C）、张（Zhang, R）、威瑟斯（Withers, S.G）、布雷耶（Brayer, G.D.）
提交日期：2009-08-04
发布日期：2009-10-27
最后修改日期：2024-11-06
实验方法：X射线衍射（X-RAY DIFFRACTION，分辨率1.43 Å）
引用：《定向"原位"抑制剂延伸策略用于结构表征人胰腺α-淀粉酶的共价糖基-酶中间体》，刊载于《生物化学》（Biochemistry），第48卷，2009年