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)

    Research output: Contribution to journalArticleScientificpeer-review

    17 Citations (Scopus)

    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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