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

doi:10.1016/0014-5793(90)81457-Y

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)

Ghent University

Research output: Contribution to journal › Article › Scientific › peer-review

19 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 language	English
Pages (from-to)	135-138
Journal	FEBS Letters
Volume	275
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(90)81457-Y
Publication status	Published - 1990
MoE publication type	A1 Journal article-refereed

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title = "Site-directed mutagenesis of the putative catalytic residues of Trichoderma reesei cellobiohydrolase I and endoglucanase I",

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.",

author = "Yasushi Mitsuishi and Sunee Nitisinprasert and Markku Saloheimo and Isa Biese and Tapani Reinikainen and Marc Claeyssens and Sirkka Ker{\"a}nen and Jonathan Knowles and Tuula Teeri",

year = "1990",

doi = "10.1016/0014-5793(90)81457-Y",

language = "English",

volume = "275",

pages = "135--138",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Wiley",

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T1 - Site-directed mutagenesis of the putative catalytic residues of Trichoderma reesei cellobiohydrolase I and endoglucanase I

AU - Mitsuishi, Yasushi

AU - Nitisinprasert, Sunee

AU - Saloheimo, Markku

AU - Biese, Isa

AU - Reinikainen, Tapani

AU - Claeyssens, Marc

AU - Keränen, Sirkka

AU - Knowles, Jonathan

AU - Teeri, Tuula

PY - 1990

Y1 - 1990

N2 - 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.

AB - 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.

U2 - 10.1016/0014-5793(90)81457-Y

DO - 10.1016/0014-5793(90)81457-Y

M3 - Article

SN - 0014-5793

VL - 275

SP - 135

EP - 138

JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -

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

Abstract

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