Engineering of a glycosidase Family 7 cellobiohydrolase to more alkaline pH optimum: the pH behaviour of Trichoderma reesei Cel7A and its E223S/ A224H/L225V/T226A/D262G mutant

The crystal structures of Family 7 glycohydrolases suggest that a histidine residue near the acid/base catalyst could account for the higher pH optimum of the Humicola insolens endoglucanase Cel7B, than the corresponding Trichoderma reesei enzymes. Modelling studies indicated that introduction of hi...

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Veröffentlicht in:	Biochemical journal 2001-05, Vol.356 (Pt 1), p.19-30
Hauptverfasser:	Becker, D, Braet, C, Brumer , 3rd, H, Claeyssens, M, Divne, C, Fagerström, B R, Harris, M, Jones, T A, Kleywegt, G J, Koivula, A, Mahdi, S, Piens, K, Sinnott, M L, Ståhlberg, J, Teeri, T T, Underwood, M, Wohlfahrt, G
Format:	Artikel
Sprache:	eng
Schlagworte:	2-chloro-4-nitrophenyl lactoside 3,4-Dinitrophenyl lactoside 7-cellobiohydrolase Alkalies Catalytic Domain - genetics Cel7A protein cellobiose Cellobiose - analogs & derivatives Cellulase - chemistry Cellulase - genetics Cellulase - metabolism Cellulose - metabolism Cellulose 1,4-beta-Cellobiosidase Crystallography, X-Ray endoglucanase endoglucanase Cel7B Enzyme Stability glycosidase Histidine Humicola insolens Hydrogen-Ion Concentration Kinetics Models, Molecular Mutation Protein Engineering Trichoderma - enzymology Trichoderma - genetics Trichoderma reesei
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