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Identification of two tryptophan residues in endoglucanase III from Trichoderma reesei essential for cellulose binding and catalytic activity
Journal article   Peer reviewed

Identification of two tryptophan residues in endoglucanase III from Trichoderma reesei essential for cellulose binding and catalytic activity

R Macarron, B Henrissat, J vanBeeuman, J M Dominguez and M Claeyssens
ENZYMATIC DEGRADATION OF INSOLUBLE CARBOHYDRATES, Vol.618, pp.164-173
ACS Symposium Series
01/01/1995

Abstract

Agriculture Agronomy Biotechnology & Applied Microbiology Chemistry Chemistry, Organic Energy & Fuels Life Sciences & Biomedicine Physical Sciences Science & Technology Technology
Three tryptophan residues are readily oxydized by N-bromosuccinimide in endoglucanase III from Trichoderma reesei. Evidence was obtained that the residue first modified (Trp(5)) is situated in the cellulose-binding domain and the second (Trp(255)) in the enzyme's catalytic site. The latter influences the binding and hydrolysis of soluble substrates and more specifically that of chromophoric cellotriosides. The modification of a third residue does not further affect the catalytic properties.

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