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)

Research output: Contribution to journalArticleScientificpeer-review

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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 languageEnglish
Pages (from-to)341-346
JournalFEBS Letters
Volume429
Issue number3
DOIs
Publication statusPublished - 1998
MoE publication typeA1 Journal article-refereed

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Cellulose 1,4-beta-Cellobiosidase
Trichoderma
Cellulose
Tryptophan
Catalytic Domain
Tunnels
Crystalline materials
Glucose
Degradation
Glucans
Mutagenesis
Enzymes
Substrates

Cite this

Koivula, Anu ; Kinnari, Tiina ; Harjunpää, Vesa ; Ruohonen, Laura ; Teleman, Anita ; Drakenberg, Torbjörn ; Rouvinen, Juha ; Jones, Alwyn ; Teeri, Tuula. / Tryptophan 272: An essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A. In: FEBS Letters. 1998 ; Vol. 429, No. 3. pp. 341-346.
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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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Koivula, A, Kinnari, T, Harjunpää, V, Ruohonen, L, Teleman, A, Drakenberg, T, Rouvinen, J, Jones, A & Teeri, T 1998, 'Tryptophan 272: An essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A', FEBS Letters, vol. 429, no. 3, pp. 341-346. https://doi.org/10.1016/S0014-5793(98)00596-1

Tryptophan 272: An essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A. / Koivula, Anu; Kinnari, Tiina; Harjunpää, Vesa; Ruohonen, Laura; Teleman, Anita; Drakenberg, Torbjörn; Rouvinen, Juha; Jones, Alwyn; Teeri, Tuula (Corresponding Author).

In: FEBS Letters, Vol. 429, No. 3, 1998, p. 341-346.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

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

VL - 429

SP - 341

EP - 346

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 3

ER -