A Novel Combination of Two Classic Catalytic Schemes

A Novel Combination of Two Classic Catalytic Schemes The crystal structure of an alkaline Bacillus cellulase catalytic core, from glucoside hydrolase family 5, reveals a novel combination of the catalytic machinery of two classic textbook enzymes. The enzyme has the expected two glutamate residues in close proximity to one another in the active-site that are typical of retaining cellulases. However, the proton donor, glutamate 139 is also unexpectedly a member of a serine-histidine-glutamate catalytic triad, forming a novel combination of catalytic machineries. Structure and sequence analysis of glucoside hydrolase family 5 reveal that the triad is highly conserved, but with variations at the equivalent of the serine position. We speculate that the purpose of this novel catalytic triad is to control the protonation of the acid/base glutamate, facilitating the first step of the catalytic reaction, protonation of the substrate, by the proton donor glutamate. If correct, this will be a novel use for a catalytic triad. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Molecular Biology Elsevier

A Novel Combination of Two Classic Catalytic Schemes

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Publisher
Elsevier
Copyright
Copyright © 2002 Elsevier Science Ltd
ISSN
0022-2836
DOI
10.1016/S0022-2836(02)00387-X
Publisher site
See Article on Publisher Site

Abstract

The crystal structure of an alkaline Bacillus cellulase catalytic core, from glucoside hydrolase family 5, reveals a novel combination of the catalytic machinery of two classic textbook enzymes. The enzyme has the expected two glutamate residues in close proximity to one another in the active-site that are typical of retaining cellulases. However, the proton donor, glutamate 139 is also unexpectedly a member of a serine-histidine-glutamate catalytic triad, forming a novel combination of catalytic machineries. Structure and sequence analysis of glucoside hydrolase family 5 reveal that the triad is highly conserved, but with variations at the equivalent of the serine position. We speculate that the purpose of this novel catalytic triad is to control the protonation of the acid/base glutamate, facilitating the first step of the catalytic reaction, protonation of the substrate, by the proton donor glutamate. If correct, this will be a novel use for a catalytic triad.

Journal

Journal of Molecular BiologyElsevier

Published: Jul 5, 2002

References

  • Molecular biology of cellulose degradation
    Beguin, P.
  • Crystallization and preliminary X-ray analysis of the major endoglucanase from Thermoascus aurantiacus
    Lo Leggio, L.; Parry, N.J.; Van Beemen, J.; Claeyssens, M.; Bhat, M.K.; Pickersgill, R.W.
  • The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism
    Dominguez, R.; Souchon, H.; Lascombe, M.; Alzari, P.M.
  • Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II
    Kryger, G.; Harel, M.; Giles, K.; Toker, L.; Velan, B.; Lazar, A.

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