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Mechanism of stabilization of Bacillus circulans xylanase upon the introduction of disulfide bonds

DOITrouver le DOI : https://doi.org/10.1016/j.bpc.2006.10.006
AuteurRechercher : ; Rechercher : 1; Rechercher : ; Rechercher :
Affiliation
  1. Conseil national de recherches Canada. Institut des sciences biologiques du CNRC
FormatTexte, Article
Sujetdisulfides; drug effects; Endo-1,4-beta Xylanases; Enzyme Stability; enzymology; LED; MUTANT; PATHWAY; Protein Denaturation; stability; Temperature
Résumé
The introduction of disulfide bonds has been used as a strategy to enhance the stability of Bacillus circulans xylanase. The transition temperature of the S100C/N148C (DS1), V98C/A152C (DS2), and A1GC/G187,C188 (cXl) in comparison to the wild type was increased by 5.0, 4.1 and 3.8 °C, respectively. Interestingly, a combination of two disulfide bonds of DS1 and cXl (cDS1, circular disulfide 1) led to a 12 °C increase in the transition temperature. Importantly, an increase in the melting point and ΔΔG values of the cDS1 mutant was cooperative. These results suggest that the mechanism of stabilization by disulfide bonds under irreversible denaturation condition is achieved through: (1) a change in the rate-limiting step on the denaturation pathway; (2) destabilizing the unfolded state without affecting the relative rate constants on the denaturation pathway (like cXl mutant); and (3) or combination of the two (cDS1 mutant).
Date de publication
Dans
  • Biophysical Chemistry 125, nº 2-3 (février 2007) : 453–461.
Langueanglais
Numéro du CNRCDAVOODI2007
DAVOODI2006
Numéro NPARC9374331
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Identificateur de l’enregistrement4707bd2b-388b-4109-ba2a-323378059d4c
Enregistrement créé2009-07-10
Enregistrement modifié2020-05-10

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