Tryptophan 272: An essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A

Anu Koivula; Tiina Kinnari; Vesa Harjunpää; Laura Ruohonen; Anita Teleman; Torbjörn Drakenberg; Juha Rouvinen; Alwyn Jones; Tuula Teeri

doi:10.1016/S0014-5793(98)00596-1

Tryptophan 272: An essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A

Anu Koivula
, Tiina Kinnari
, Vesa Harjunpää
, Laura Ruohonen
, Anita Teleman
, Torbjörn Drakenberg
, Juha Rouvinen
, Alwyn Jones
, Tuula Teeri^*

^*Corresponding author for this work

VTT Technical Research Centre of Finland

VTT (former employee or external)
Uppsala University

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

108 Citations (Scopus)

Abstract

Trichoderma reesei cellobiohydrolase Cel6A (formerly CBHII) has a tunnel shaped active site with four internal subsites for the glucose units. We have predicted an additional ring stacking interaction for a sixth glucose moiety with a tryptophan residue (W272) found on the domain surface. Mutagenesis of this residue selectively impairs the enzyme function on crystalline cellulose but not on soluble or amorphous substrates. Our data shows that W272 forms an additional subsite at the entrance of the active site tunnel and suggests it has a specialised role in crystalline cellulose degradation, possibly in guiding a glucan chain into the tunnel.

Original language	English
Pages (from-to)	341-346
Journal	FEBS Letters
Volume	429
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(98)00596-1
Publication status	Published - 1998
MoE publication type	A1 Journal article-refereed

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10.1016/S0014-5793(98)00596-1

Corrigendum to: Tryptophan 272: An essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A (FEBS 20361) [FEBS Letters 429 (1998) (341-346] PII: S0014579398005961)
Koivula, A., Kinnari, T., Harjunpaa, V., Ruohonen, L., Teleman, A., Drakenberg, T., Rouvinen, J., Jones, T. A. & Teeri, T. T., 1 Jan 1999, In: FEBS Letters. 447, 2-3, 1 p.
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title = "Tryptophan 272: An essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A",

abstract = "Trichoderma reesei cellobiohydrolase Cel6A (formerly CBHII) has a tunnel shaped active site with four internal subsites for the glucose units. We have predicted an additional ring stacking interaction for a sixth glucose moiety with a tryptophan residue (W272) found on the domain surface. Mutagenesis of this residue selectively impairs the enzyme function on crystalline cellulose but not on soluble or amorphous substrates. Our data shows that W272 forms an additional subsite at the entrance of the active site tunnel and suggests it has a specialised role in crystalline cellulose degradation, possibly in guiding a glucan chain into the tunnel.",

author = "Anu Koivula and Tiina Kinnari and Vesa Harjunp{\"a}{\"a} and Laura Ruohonen and Anita Teleman and Torbj{\"o}rn Drakenberg and Juha Rouvinen and Alwyn Jones and Tuula Teeri",

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pages = "341--346",

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T1 - Tryptophan 272: An essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A

AU - Koivula, Anu

AU - Kinnari, Tiina

AU - Harjunpää, Vesa

AU - Ruohonen, Laura

AU - Teleman, Anita

AU - Drakenberg, Torbjörn

AU - Rouvinen, Juha

AU - Jones, Alwyn

AU - Teeri, Tuula

PY - 1998

Y1 - 1998

N2 - Trichoderma reesei cellobiohydrolase Cel6A (formerly CBHII) has a tunnel shaped active site with four internal subsites for the glucose units. We have predicted an additional ring stacking interaction for a sixth glucose moiety with a tryptophan residue (W272) found on the domain surface. Mutagenesis of this residue selectively impairs the enzyme function on crystalline cellulose but not on soluble or amorphous substrates. Our data shows that W272 forms an additional subsite at the entrance of the active site tunnel and suggests it has a specialised role in crystalline cellulose degradation, possibly in guiding a glucan chain into the tunnel.

AB - Trichoderma reesei cellobiohydrolase Cel6A (formerly CBHII) has a tunnel shaped active site with four internal subsites for the glucose units. We have predicted an additional ring stacking interaction for a sixth glucose moiety with a tryptophan residue (W272) found on the domain surface. Mutagenesis of this residue selectively impairs the enzyme function on crystalline cellulose but not on soluble or amorphous substrates. Our data shows that W272 forms an additional subsite at the entrance of the active site tunnel and suggests it has a specialised role in crystalline cellulose degradation, possibly in guiding a glucan chain into the tunnel.

U2 - 10.1016/S0014-5793(98)00596-1

DO - 10.1016/S0014-5793(98)00596-1

M3 - Article

SN - 0014-5793

VL - 429

SP - 341

EP - 346

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

Tryptophan 272: An essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A

Abstract

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Corrigendum to: Tryptophan 272: An essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A (FEBS 20361) [FEBS Letters 429 (1998) (341-346] PII: S0014579398005961)

Cite this