The difference in affinity between two fungal cellulose-binding domains is dominated by a single amino acid substitution

Markus Linder; Gunnar Lindeberg; Tapani Reinikainen; Tuula Teeri; Göran Pettersson

doi:10.1016/0014-5793(95)00961-8

The difference in affinity between two fungal cellulose-binding domains is dominated by a single amino acid substitution

Markus Linder (Corresponding Author), Gunnar Lindeberg, Tapani Reinikainen, Tuula Teeri, Göran Pettersson

VTT Technical Research Centre of Finland

Uppsala University

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

102 Citations (Scopus)

Abstract

Cellulose‐binding domains (CBDs) form distinct functional units of most cellulolytic enzymes. We have compared the cellulose‐binding affinities of the CBDs of cellobiohydrolase I (CBHI) and endoglucanase I (EGI) from the fungus Trichoderma reesei. The CBD of EGI had significantly higher affinity than that of CBHI. Four variants of the CBHI CBD were made in order to identify the residues responsible for the increased affinity in EGI. Most of the difference could be ascribed to a replacement of a tyrosine by a tryptophan on the flat cellulose‐binding face.

Original language	English
Pages (from-to)	96-98
Journal	FEBS Letters
Volume	372
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(95)00961-8
Publication status	Published - 1995
MoE publication type	A1 Journal article-refereed

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title = "The difference in affinity between two fungal cellulose-binding domains is dominated by a single amino acid substitution",

abstract = "Cellulose‐binding domains (CBDs) form distinct functional units of most cellulolytic enzymes. We have compared the cellulose‐binding affinities of the CBDs of cellobiohydrolase I (CBHI) and endoglucanase I (EGI) from the fungus Trichoderma reesei. The CBD of EGI had significantly higher affinity than that of CBHI. Four variants of the CBHI CBD were made in order to identify the residues responsible for the increased affinity in EGI. Most of the difference could be ascribed to a replacement of a tyrosine by a tryptophan on the flat cellulose‐binding face.",

author = "Markus Linder and Gunnar Lindeberg and Tapani Reinikainen and Tuula Teeri and G{\"o}ran Pettersson",

note = "Project code: B5SU00132",

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T1 - The difference in affinity between two fungal cellulose-binding domains is dominated by a single amino acid substitution

AU - Linder, Markus

AU - Lindeberg, Gunnar

AU - Reinikainen, Tapani

AU - Teeri, Tuula

AU - Pettersson, Göran

N1 - Project code: B5SU00132

PY - 1995

Y1 - 1995

N2 - Cellulose‐binding domains (CBDs) form distinct functional units of most cellulolytic enzymes. We have compared the cellulose‐binding affinities of the CBDs of cellobiohydrolase I (CBHI) and endoglucanase I (EGI) from the fungus Trichoderma reesei. The CBD of EGI had significantly higher affinity than that of CBHI. Four variants of the CBHI CBD were made in order to identify the residues responsible for the increased affinity in EGI. Most of the difference could be ascribed to a replacement of a tyrosine by a tryptophan on the flat cellulose‐binding face.

AB - Cellulose‐binding domains (CBDs) form distinct functional units of most cellulolytic enzymes. We have compared the cellulose‐binding affinities of the CBDs of cellobiohydrolase I (CBHI) and endoglucanase I (EGI) from the fungus Trichoderma reesei. The CBD of EGI had significantly higher affinity than that of CBHI. Four variants of the CBHI CBD were made in order to identify the residues responsible for the increased affinity in EGI. Most of the difference could be ascribed to a replacement of a tyrosine by a tryptophan on the flat cellulose‐binding face.

U2 - 10.1016/0014-5793(95)00961-8

DO - 10.1016/0014-5793(95)00961-8

M3 - Article

SN - 0014-5793

VL - 372

SP - 96

EP - 98

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

The difference in affinity between two fungal cellulose-binding domains is dominated by a single amino acid substitution

Abstract

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