1hx0: Difference between revisions

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{{Seed}}
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{{STRUCTURE_1hx0|  PDB=1hx0  |  SCENE=  }}  
{{STRUCTURE_1hx0|  PDB=1hx0  |  SCENE=  }}  


'''STRUCTURE OF PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE "TRUNCATE" ACARBOSE MOLECULE (PSEUDOTRISACCHARIDE)'''
===STRUCTURE OF PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE "TRUNCATE" ACARBOSE MOLECULE (PSEUDOTRISACCHARIDE)===




==Overview==
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Mammalian alpha-amylases catalyze the hydrolysis of alpha-linked glucose polymers according to a complex processive mechanism. We have determined the X-ray structures of porcine pancreatic alpha-amylase complexes with the smallest molecule of the trestatin family (acarviosine-glucose) which inhibits porcine pancreatic alpha-amylase and yet is not hydrolyzed by the enzyme. A structure analysis at 1.38 A resolution of this complex allowed for a clear identification of a genuine single hexasaccharide species composed of two alpha-1,4-linked original molecules bound to the active site of the enzyme. The structural results supported by mass spectrometry experiments provide evidence for an enzymatically catalyzed condensation reaction in the crystal.
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{{ABSTRACT_PUBMED_11412124}}


==About this Structure==
==About this Structure==
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[[Category: Inhibitor]]
[[Category: Inhibitor]]
[[Category: Pancrea]]
[[Category: Pancrea]]
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