1U33
In situ extension as an approach for identifying novel alpha-amylase inhibitors
Summary for 1U33
| Entry DOI | 10.2210/pdb1u33/pdb |
| Related | 1U2Y 1U30 |
| Descriptor | Alpha-amylase, pancreatic, 2-acetamido-2-deoxy-beta-D-glucopyranose, 4'-O-METHYL-MALTOSYL-ALPHA (1,4)-(Z, 3S,4S,5R,6R)-3,4,5-TRIHYDROXY-6-HYDROXYMETHYL-PIPERIDIN-2-ONE, ... (6 entities in total) |
| Functional Keywords | glycosidase, human pancreatic alpha-amylase, acarbose, inhibitor, glucosidase, enzyme mechanism, hydrolase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 56758.52 |
| 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 citation | Numao, 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: 15304511DOI: 10.1074/jbc.M406804200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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