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Structural and mechanistic studies of chloride induced activation of human pancreatic alpha-amylase.

Maurus R, Begum A, Kuo HH, Racaza A, Numao S, Andersen C, Tams JW, Vind J, Overall CM, Withers SG, Brayer GD
Protein Sci 14 743-55 (2005)
Related entries: 1xgz, 1xh1, 1xh2

Cited: 26 times
EuropePMC logo PMID: 15722449

Abstract

The mechanism of allosteric activation of alpha-amylase by chloride has been studied through structural and kinetic experiments focusing on the chloride-dependent N298S variant of human pancreatic alpha-amylase (HPA) and a chloride-independent TAKA-amylase. Kinetic analysis of the HPA variant clearly demonstrates the pronounced activating effect of chloride ion binding on reaction rates and its effect on the pH-dependence of catalysis. Structural alterations observed in the N298S variant upon chloride ion binding suggest that the chloride ion plays a variety of roles that serve to promote catalysis. One of these is having a strong influence on the positioning of the acid/base catalyst residue E233. Absence of chloride ion results in multiple conformations for this residue and unexpected enzymatic products. Chloride ion and N298 also appear to stabilize a helical region of polypeptide chain from which projects the flexible substrate binding loop unique to chloride-dependent alpha-amylases. This structural feature also serves to properly orient the catalytically essential residue D300. Comparative analyses show that the chloride-independent alpha-amylases compensate for the absence of bound chloride by substituting a hydrophobic core, altering the manner in which substrate interactions are made and shifting the placement of N298. These evolutionary differences presumably arise in response to alternative operating environments or the advantage gained in a particular product profile. Attempts to engineer chloride-dependence into the chloride-independent TAKA-amylase point out the complexity of this system, and the fact that a multitude of factors play a role in binding chloride ion in the chloride-dependent alpha-amylases.

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  2. Luminal substrate "brake" on mucosal maltase-glucoamylase activity regulates total rate of starch digestion to glucose. Quezada-Calvillo R, Robayo-Torres CC, Ao Z, Hamaker BR, Quaroni A, Brayer GD, Sterchi EE, Baker SS, Nichols BL. J Pediatr Gastroenterol Nutr 45 32-43 (2007)
  3. High lumenal chloride in the lysosome is critical for lysosome function. Chakraborty K, Leung K, Krishnan Y. Elife 6 e28862 (2017)
  4. The structure of the Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding mode. Caner S, Nguyen N, Aguda A, Zhang R, Pan YT, Withers SG, Brayer GD. Glycobiology 23 1075-1083 (2013)
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  6. Digestive alpha-amylases of the flour moth Ephestia kuehniella--adaptation to alkaline environment and plant inhibitors. Pytelková J, Hubert J, Lepsík M, Sobotník J, Sindelka R, Krízková I, Horn M, Mares M. FEBS J 276 3531-3546 (2009)
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  8. Group B streptococcus pullulanase crystal structures in the context of a novel strategy for vaccine development. Gourlay LJ, Santi I, Pezzicoli A, Grandi G, Soriani M, Bolognesi M. J Bacteriol 191 3544-3552 (2009)
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  14. 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)
  15. Chloride to the rescue. Newcomer ME. J Biol Chem 294 11402-11403 (2019)
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  17. 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)
  18. Purification and characterization of a chloride ion-dependent α-glucosidase from the midgut gland of Japanese scallop (Patinopecten yessoensis). Masuda Y, Okuyama M, Iizuka T, Nakai H, Saburi W, Fukukawa T, Maneesan J, Tagami T, Naraoka T, Mori H, Kimura A. Biosci Biotechnol Biochem 80 479-485 (2016)
  19. Electrolyte imbalance causes suppression of NK and T cell effector function in malignant ascites. Hrvat A, Schmidt M, Wagner B, Zwanziger D, Kimmig R, Volbracht L, Brandau S, Mallmann-Gottschalk N. J Exp Clin Cancer Res 42 235 (2023)
  20. Functional role of R462 in the degradation of hyaluronan catalyzed by hyaluronate lyase from Streptococcus pneumoniae. Li F, Xu D. J Mol Model 21 196 (2015)
  21. Reflection on design and testing of pancreatic alpha-amylase inhibitors: an in silico comparison between rat and rabbit enzyme models. Khalil-Moghaddam S, Ebrahim-Habibi A, Pasalar P, Yaghmaei P, Hayati-Roodbari N. Daru 20 77 (2012)
  22. Structural and Functional Characterization of Drosophila melanogaster α-Amylase. Rhimi M, Da Lage JL, Haser R, Feller G, Aghajari N. Molecules 28 5327 (2023)
  23. Syntheses, in vitro, and in silico studies of rhodanine-based schiff bases as potential α-amylase inhibitors and radicals (DPPH and ABTS) scavengers. Egu SA, Ali I, Khan KM, Chigurupati S, Qureshi U, Salar U, Taha M, Felemban SG, Venugopal V, Ul-Haq Z. Mol Divers 27 767-791 (2023)


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