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

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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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Cellulose 1,4-beta-Cellobiosidase
Cellulases
Mutagenesis
Trichoderma
Site-Directed Mutagenesis
Enzymes
Protons
Catalytic Domain
Yeasts
Yeast

Cite this

Mitsuishi, Yasushi ; Nitisinprasert, Sunee ; Saloheimo, Markku ; Biese, Isa ; Reinikainen, Tapani ; Claeyssens, Marc ; Keränen, Sirkka ; Knowles, Jonathan ; Teeri, Tuula. / Site-directed mutagenesis of the putative catalytic residues of Trichoderma reesei cellobiohydrolase I and endoglucanase I. In: FEBS Letters. 1990 ; Vol. 275, No. 1-2. pp. 135-138.
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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",
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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, vol. 275, no. 1-2, pp. 135-138. https://doi.org/10.1016/0014-5793(90)81457-Y

Site-directed mutagenesis of the putative catalytic residues of Trichoderma reesei cellobiohydrolase I and endoglucanase I. / Mitsuishi, Yasushi; Nitisinprasert, Sunee; Saloheimo, Markku; Biese, Isa; Reinikainen, Tapani; Claeyssens, Marc; Keränen, Sirkka; Knowles, Jonathan; Teeri, Tuula (Corresponding Author).

In: FEBS Letters, Vol. 275, No. 1-2, 1990, p. 135-138.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

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

VL - 275

SP - 135

EP - 138

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1-2

ER -