Site-directed mutagenesis of the putative catalytic residues of Trichoderma reesei cellobiohydrolase I and endoglucanase I

Yasushi Mitsuishi, Sunee Nitisinprasert, Markku Saloheimo, Isa Biese, Tapani Reinikainen, Marc Claeyssens, Sirkka Keränen, Jonathan Knowles, Tuula Teeri (Corresponding Author)

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Abstract

Site directed mutagenesis has been performed to test hypotheses concerning the putative active sites of Trichoderma reesci cellobiohydrolase I and endoglucanase I. It is shown that mutagenesis of the residue 1:126, previously proposed to be the proton donor in CBHI, did not totally inactive the enzyme while mutagenesis of the residue 1:127 in the homologous enzyme EG1 resulted in complete loss of activity. These results are compared with those obtained in similar studies of other glucanases and the effects on enzymatic activity of hyperglycosylation of the yeast produced cellulases are discussed.

Original languageEnglish
Pages (from-to)135-138
JournalFEBS Letters
Volume275
Issue number1-2
DOIs
Publication statusPublished - 1990
MoE publication typeA1 Journal article-refereed

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    Mitsuishi, Y., Nitisinprasert, S., Saloheimo, M., Biese, I., Reinikainen, T., Claeyssens, M., Keränen, S., Knowles, J., & Teeri, T. (1990). Site-directed mutagenesis of the putative catalytic residues of Trichoderma reesei cellobiohydrolase I and endoglucanase I. FEBS Letters, 275(1-2), 135-138. https://doi.org/10.1016/0014-5793(90)81457-Y