Structural highlights
5emy is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , |
| NonStd Res: | |
| Related: | 4x9y, 4w93, 1cpu |
| Gene: | AMY2A (HUMAN) |
| Activity: | Alpha-amylase, with EC number 3.2.1.1 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Publication Abstract from PubMed
As part of a search for selective, mechanism-based covalent inhibitors of human pancreatic alpha-amylase we describe the chemoenzymatic synthesis of the disaccharide analog alpha-glucosyl epi-cyclophellitol, demonstrate its stoichiometric reaction with human pancreatic alpha-amylase and evaluate the time dependence of its inhibition. X-ray crystallographic analysis of the covalent derivative so formed confirms its reaction at the active site with formation of a covalent bond to the catalytic nucleophile D197. The structure illuminates the interactions with the active site and confirms OH4' on the nonreducing end sugar as a good site for attachment of fluorescent tags in generating probes for localization and quantitation of amylase in vivo.
Glucosyl epi-cyclophellitol allows mechanism-based inactivation and structural analysis of human pancreatic alpha-amylase.,Caner S, Zhang X, Jiang J, Chen HM, Nguyen NT, Overkleeft H, Brayer GD, Withers SG FEBS Lett. 2016 Apr;590(8):1143-51. doi: 10.1002/1873-3468.12143. Epub 2016 Apr, 3. PMID:27000970[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Caner S, Zhang X, Jiang J, Chen HM, Nguyen NT, Overkleeft H, Brayer GD, Withers SG. Glucosyl epi-cyclophellitol allows mechanism-based inactivation and structural analysis of human pancreatic alpha-amylase. FEBS Lett. 2016 Apr;590(8):1143-51. doi: 10.1002/1873-3468.12143. Epub 2016 Apr, 3. PMID:27000970 doi:http://dx.doi.org/10.1002/1873-3468.12143
