1hx0: Difference between revisions

Revision as of 10:03, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1hx0.png

Template:STRUCTURE 1hx0

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)

Template:ABSTRACT PUBMED 11412124

About this StructureAbout this Structure

1HX0 is a Single protein structure of sequence from Sus scrofa. 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

Page seeded by OCA on Tue Jul 1 10:02:57 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''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==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11412124}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11412124 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11412124}}
 ==About this Structure==
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 [[Category: Inhibitor]]
 [[Category: Pancrea]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:18:42 2008''
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