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1U2Y

In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing D-gluconhydroximo-1,5-lactam

Summary for 1U2Y
Entry DOI10.2210/pdb1u2y/pdb
Related1CPU 1U30 1U33
DescriptorAlpha-amylase, pancreatic, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
Functional Keywordsglycosidase, human pancreatic alpha-amylase, acarbose, inhibitor, glucosidase, enzyme mechanism, hydrolase
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight56420.21
Authors
Numao, S.,Li, C.,Damager, I.,Wrodnigg, T.M.,Begum, A.,Overall, C.M.,Brayer, G.D.,Withers, S.G. (deposition date: 2004-07-20, release date: 2004-09-07, Last modification date: 2024-10-16)
Primary citationNumao, S.,Damager, I.,Li, C.,Wrodnigg, T.M.,Begum, A.,Overall, C.M.,Brayer, G.D.,Withers, S.G.
In Situ Extension as an Approach for Identifying Novel alpha-Amylase Inhibitors.
J.Biol.Chem., 279:48282-48291, 2004
Cited by
PubMed Abstract: A new approach for the discovery and subsequent structural elucidation of oligosaccharide-based inhibitors of alpha-amylases based upon autoglucosylation of known alpha-glucosidase inhibitors is presented. This concept, highly analogous to what is hypothesized to occur with acarbose, is demonstrated with the known alpha-glucosidase inhibitor, d-gluconohydroximino-1,5-lactam. This was transformed from an inhibitor of human pancreatic alpha-amylase with a K(i) value of 18 mm to a trisaccharide analogue with a K(i) value of 25 mum. The three-dimensional structure of this complex was determined by x-ray crystallography and represents the first such structure determined with this class of inhibitors in any alpha-glycosidase. This approach to the discovery and structural analysis of amylase inhibitors should be generally applicable to other endoglucosidases and readily adaptable to a high throughput format.
PubMed: 15304511
DOI: 10.1074/jbc.M406804200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

227561

数据于2024-11-20公开中

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