Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial enzyme 1 1 Edited by R. Huber

Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial... The crystal structure of the catalytic domain of alkaline cellulase K was determined at 1.9 Å resolution. Because of the most alkaliphilic nature and it’s highest activity at pH 9.5, it is used commercially in laundry detergents. An analysis of the structural bases of the alkaliphilic character of the enzyme suggested a mechanism similar to that previously proposed for alkaline proteases, that is, an increase in the number of Arg, His, and Gln residues, and a decrease in Asp and Lys residues. Some ion pairs were formed by the gained Arg residues, which is similar to what has been found in the alkaline proteases. Lys-Asp ion pairs are disfavored and partly replaced with Arg-Asp ion pairs. The alkaline adaptation appeared to be a remodeling of ion pairs so that the charge balance is kept in the high pH range. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Molecular Biology Elsevier

Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial enzyme 1 1 Edited by R. Huber

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Publisher
Elsevier
Copyright
Copyright © 2001 Academic Press
ISSN
0022-2836
DOI
10.1006/jmbi.2001.4835
Publisher site
See Article on Publisher Site

Abstract

The crystal structure of the catalytic domain of alkaline cellulase K was determined at 1.9 Å resolution. Because of the most alkaliphilic nature and it’s highest activity at pH 9.5, it is used commercially in laundry detergents. An analysis of the structural bases of the alkaliphilic character of the enzyme suggested a mechanism similar to that previously proposed for alkaline proteases, that is, an increase in the number of Arg, His, and Gln residues, and a decrease in Asp and Lys residues. Some ion pairs were formed by the gained Arg residues, which is similar to what has been found in the alkaline proteases. Lys-Asp ion pairs are disfavored and partly replaced with Arg-Asp ion pairs. The alkaline adaptation appeared to be a remodeling of ion pairs so that the charge balance is kept in the high pH range.

Journal

Journal of Molecular BiologyElsevier

Published: Jul 27, 2001

References

  • Insight into ligand-induced conformational change in Cel5A from Bacillus agaradhaerens revealed by a catalytically active crystal form
    Varrot, A; Schůlein, M; Davies, G.J
  • The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit active mechanism
    Dominguez, R; Souchon, H; Lascombe, M.-B; Alzari, P.M
  • PROCHECK
    Laskowski, R.A

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