Enzyme-Catalyzed Condensation Reaction in a Mammalian -Amylase. High-Resolution Structural Analysis of an Enzyme-Inhibitor Complex
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- 作者：Minxie Qian ; Virginie Nahoum ; Jacques Bonicel ; Hilmar Bischoff ; Bernard Henrissat ; and Franç ; oise Payan
- 刊名：Biochemistry
- 出版年：2001
- 出版时间：June 26, 2001
- 年：2001
- 卷：40
- 期：25
- 页码：7700 - 7709
- 全文大小：316K
- 年卷期：v.40,no.25(June 26, 2001)
- ISSN：1520-4995
文摘
Mammalian 
-amylases catalyze the hydrolysis of -linked glucose polymers according to acomplex processive mechanism. We have determined the X-ray structures of porcine pancreatic -amylasecomplexes with the smallest molecule of the trestatin family (acarviosine-glucose) which inhibits porcinepancreatic -amylase and yet is not hydrolyzed by the enzyme. A structure analysis at 1.38 Å resolutionof this complex allowed for a clear identification of a genuine single hexasaccharide species composedof two -1,4-linked original molecules bound to the active site of the enzyme. The structural resultssupported by mass spectrometry experiments provide evidence for an enzymatically catalyzed condensationreaction in the crystal.
-amylases catalyze the hydrolysis of -linked glucose polymers according to acomplex processive mechanism. We have determined the X-ray structures of porcine pancreatic -amylasecomplexes with the smallest molecule of the trestatin family (acarviosine-glucose) which inhibits porcinepancreatic -amylase and yet is not hydrolyzed by the enzyme. A structure analysis at 1.38 Å resolutionof this complex allowed for a clear identification of a genuine single hexasaccharide species composedof two -1,4-linked original molecules bound to the active site of the enzyme. The structural resultssupported by mass spectrometry experiments provide evidence for an enzymatically catalyzed condensationreaction in the crystal.