1hx0
STRUCTURE OF PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE "TRUNCATE" ACARBOSE MOLECULE (PSEUDOTRISACCHARIDE)
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OverviewOverview
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.
About this StructureAbout this Structure
1HX0 is a Single protein structure of sequence from Sus scrofa with MAL, CL, CA and EDO as ligands. Active as Alpha-amylase, with EC number 3.2.1.1 Full crystallographic information is available from OCA.
ReferenceReference
Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex., Qian M, Nahoum V, Bonicel J, Bischoff H, Henrissat B, Payan F, Biochemistry. 2001 Jun 26;40(25):7700-9. PMID:11412124
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