|1wo2, resolution 2.01Å ()|
|Ligands:||, , , ,|
Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion
Pig pancreatic alpha-amylase (PPA), an enzyme belonging to the alpha-amylase family, is involved in the degradation of starch. Like some other members of this family, PPA requires chloride to reach maximum activity levels. To further explain the mechanism of chloride activation, a crystal of wild-type PPA soaked with maltopentaose using a chloride-free buffer was analyzed by X-ray crystallography. A conspicuous reorientation of the acid/base catalyst Glu233 residue was found to occur. The structural results, along with kinetic data, show that the acid/base catalyst is maintained in the active site, in an optimum position, pointing toward the scissile bond-atom, due to the presence of chloride ions. The present study therefore explains the mechanism of PPA activation by chloride ions.
Molecular basis of the effects of chloride ion on the acid-base catalyst in the mechanism of pancreatic alpha-amylase., Qian M, Ajandouz el H, Payan F, Nahoum V, Biochemistry. 2005 Mar 8;44(9):3194-201. PMID:15736930
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Qian M, Ajandouz el H, Payan F, Nahoum V. Molecular basis of the effects of chloride ion on the acid-base catalyst in the mechanism of pancreatic alpha-amylase. Biochemistry. 2005 Mar 8;44(9):3194-201. PMID:15736930 doi:10.1021/bi048201t
- Qian M, Nahoum V, Bonicel J, Bischoff H, Henrissat B, Payan F. Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex. Biochemistry. 2001 Jun 26;40(25):7700-9. PMID:11412124