spacer
spacer

PDBsum entry 1wo2

Go to PDB code: 
Top Page protein ligands metals links
Hydrolase PDB id
1wo2
Jmol
Contents
Protein chain
496 a.a.
Ligands
GLC-GLC-BGC ×2
GLC-BGC
EDO ×6
Metals
_CL
_CA
Waters ×749

References listed in PDB file
Key reference
Title Molecular basis of the effects of chloride ion on the acid-Base catalyst in the mechanism of pancreatic alpha-Amylase.
Authors M.Qian, E.L. .H.Ajandouz, F.Payan, V.Nahoum.
Ref. Biochemistry, 2005, 44, 3194-3201. [DOI no: 10.1021/bi048201t]
PubMed id 15736930
Abstract
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.
Secondary reference #1
Title Enzyme-Catalyzed condensation reaction in a mammalian alpha-Amylase. High-Resolution structural analysis of an enzyme-Inhibitor complex.
Authors M.Qian, V.Nahoum, J.Bonicel, H.Bischoff, B.Henrissat, F.Payan.
Ref. Biochemistry, 2001, 40, 7700-7709.
PubMed id 11412124
Abstract
Secondary reference #2
Title Crystal structure of the pig pancreatic alpha-Amylase complexed with malto-Oligosaccharides.
Authors F.Payan, M.Qian.
Ref. J Protein Chem, 2003, 22, 275-284.
PubMed id 12962327
Abstract
PROCHECK
Go to PROCHECK summary
 Headers