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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 44 3194-201 (2005)
Related entries: 1hx0, 1ua3

Cited: 12 times
EuropePMC logo PMID: 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.

Articles citing this publication (12)

  1. Temperature adaptations in psychrophilic, mesophilic and thermophilic chloride-dependent alpha-amylases. Cipolla A, Delbrassine F, Da Lage JL, Feller G. Biochimie 94 1943-1950 (2012)
  2. Where do animal alpha-amylases come from? An interkingdom trip. Da Lage JL, Danchin EG, Casane D. FEBS Lett. 581 3927-3935 (2007)
  3. Activated effect of lignin on α-amylase. Zhang J, Cui JH, Yin T, Sun L, Li G. Food Chem 141 2229-2237 (2013)
  4. X-ray crystallographic analyses of pig pancreatic alpha-amylase with limit dextrin, oligosaccharide, and alpha-cyclodextrin. Larson SB, Day JS, McPherson A. Biochemistry 49 3101-3115 (2010)
  5. Cloning and expression analysis of the Bombyx mori α-amylase gene (Amy) from the indigenous Thai silkworm strain, Nanglai. Ngernyuang N, Kobayashi I, Promboon A, Ratanapo S, Tamura T, Ngernsiri L. J. Insect Sci. 11 38 (2011)
  6. Comprehensive enzymatic analysis of the amylolytic system in the digestive fluid of the sea hare, Aplysia kurodai: Unique properties of two α-amylases and two α-glucosidases. Tsuji A, Nishiyama N, Ohshima M, Maniwa S, Kuwamura S, Shiraishi M, Yuasa K. FEBS Open Bio 4 560-570 (2014)
  7. Interaction of europium and curium with alpha-amylase. Barkleit A, Heller A, Ikeda-Ohno A, Bernhard G. Dalton Trans 45 8724-8733 (2016)
  8. Mutation in the substrate-binding site of aminopeptidase B confers new enzymatic properties. Pham VL, Gouzy-Darmon C, Pernier J, Hanquez C, Hook V, Beinfeld MC, Nicolas P, Etchebest C, Foulon T, Cadel S. Biochimie 93 730-741 (2011)
  9. The noncatalytic triad of alpha-amylases: a novel structural motif involved in conformational stability. Marx JC, Poncin J, Simorre JP, Ramteke PW, Feller G. Proteins 70 320-328 (2008)
  10. Improving the convergence rate of a hybrid input-output phasing algorithm by varying the reflection data weight. He H, Su WP. Acta Crystallogr A Found Adv 74 36-43 (2018)
  11. In Silico Analysis of Fungal and Chloride-Dependent α-Amylases within the Family GH13 with Identification of Possible Secondary Surface-Binding Sites. Janíčková Z, Janeček Š. Molecules 26 5704 (2021)
  12. Structures of PspAG97A α-glucoside hydrolase reveal a novel mechanism for chloride induced activation. He C, Li J, Li W, Xue Y, Fang Z, Fang W, Zhang X, Wang X, Xiao Y. J. Struct. Biol. 196 426-436 (2016)


Related citations provided by authors (2)

  1. Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex.. Qian M, Nahoum V, Bonicel J, Bischoff H, Henrissat B, Payan F Biochemistry 40 7700-9 (2001)
  2. Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaccharides.. Payan F, Qian M J Protein Chem 22 275-84 (2003)

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