Modes of action of two Trichoderma reesei cellobiohydrolases

Tuula T. Teeri, Anu Koivula, Markus Linder, Tapani Reinikainen, Laura Ruohonen, Malee Srisodsuk, Marc Claeyssens, T. Alwyn Jones

Research output: Contribution to journalArticleScientificpeer-review

11 Citations (Scopus)

Abstract

Trichoderma reesei degrades native cellulose utilizing a set of cellulolytic enzymes dominated by two cellobiohydrolases, CBHI and CBHII. These enzymes exhibit the typical two domain architecture of fungal cellulases, and both act primarily as exoglucanases liberating cellobiose from the ends of the polymeric cellulose chains. The three dimensional structures of the catalytic domains of CBHI and CBHII revealed that their active sites are situated in tunnels formed by long loops on the enzymes surface. The active sites of homologous endoglucanases lack these loops and have more open active sites permitting catalytic activity in the internal positions of cellulose chains. Site-directed mutagenesis and structural studies have identified the key catalytic residues of both CBHI and CBHII. Similarly, the primary interaction surface of the cellulose-binding domain has been defined and residues responsible for its tight binding to cellulose identified.

Original languageEnglish
Pages (from-to)211-224
Number of pages14
JournalProgress in Biotechnology
Volume10
DOIs
Publication statusPublished - 1 Jan 1995
MoE publication typeA1 Journal article-refereed

Fingerprint

Cellulose 1,4-beta-Cellobiosidase
Trichoderma
Cellulose
Catalytic Domain
Enzymes
Cellobiose
Cellulases
Cellulase
Site-Directed Mutagenesis

Cite this

Teeri, T. T., Koivula, A., Linder, M., Reinikainen, T., Ruohonen, L., Srisodsuk, M., ... Alwyn Jones, T. (1995). Modes of action of two Trichoderma reesei cellobiohydrolases. Progress in Biotechnology, 10, 211-224. https://doi.org/10.1016/S0921-0423(06)80105-X
Teeri, Tuula T. ; Koivula, Anu ; Linder, Markus ; Reinikainen, Tapani ; Ruohonen, Laura ; Srisodsuk, Malee ; Claeyssens, Marc ; Alwyn Jones, T. / Modes of action of two Trichoderma reesei cellobiohydrolases. In: Progress in Biotechnology. 1995 ; Vol. 10. pp. 211-224.
@article{e3e054cc5d5d4a4d8dbb055ee3343bf2,
title = "Modes of action of two Trichoderma reesei cellobiohydrolases",
abstract = "Trichoderma reesei degrades native cellulose utilizing a set of cellulolytic enzymes dominated by two cellobiohydrolases, CBHI and CBHII. These enzymes exhibit the typical two domain architecture of fungal cellulases, and both act primarily as exoglucanases liberating cellobiose from the ends of the polymeric cellulose chains. The three dimensional structures of the catalytic domains of CBHI and CBHII revealed that their active sites are situated in tunnels formed by long loops on the enzymes surface. The active sites of homologous endoglucanases lack these loops and have more open active sites permitting catalytic activity in the internal positions of cellulose chains. Site-directed mutagenesis and structural studies have identified the key catalytic residues of both CBHI and CBHII. Similarly, the primary interaction surface of the cellulose-binding domain has been defined and residues responsible for its tight binding to cellulose identified.",
author = "Teeri, {Tuula T.} and Anu Koivula and Markus Linder and Tapani Reinikainen and Laura Ruohonen and Malee Srisodsuk and Marc Claeyssens and {Alwyn Jones}, T.",
year = "1995",
month = "1",
day = "1",
doi = "10.1016/S0921-0423(06)80105-X",
language = "English",
volume = "10",
pages = "211--224",
journal = "Progress in Biotechnology",
issn = "0921-0423",
publisher = "Elsevier",

}

Teeri, TT, Koivula, A, Linder, M, Reinikainen, T, Ruohonen, L, Srisodsuk, M, Claeyssens, M & Alwyn Jones, T 1995, 'Modes of action of two Trichoderma reesei cellobiohydrolases', Progress in Biotechnology, vol. 10, pp. 211-224. https://doi.org/10.1016/S0921-0423(06)80105-X

Modes of action of two Trichoderma reesei cellobiohydrolases. / Teeri, Tuula T.; Koivula, Anu; Linder, Markus; Reinikainen, Tapani; Ruohonen, Laura; Srisodsuk, Malee; Claeyssens, Marc; Alwyn Jones, T.

In: Progress in Biotechnology, Vol. 10, 01.01.1995, p. 211-224.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Modes of action of two Trichoderma reesei cellobiohydrolases

AU - Teeri, Tuula T.

AU - Koivula, Anu

AU - Linder, Markus

AU - Reinikainen, Tapani

AU - Ruohonen, Laura

AU - Srisodsuk, Malee

AU - Claeyssens, Marc

AU - Alwyn Jones, T.

PY - 1995/1/1

Y1 - 1995/1/1

N2 - Trichoderma reesei degrades native cellulose utilizing a set of cellulolytic enzymes dominated by two cellobiohydrolases, CBHI and CBHII. These enzymes exhibit the typical two domain architecture of fungal cellulases, and both act primarily as exoglucanases liberating cellobiose from the ends of the polymeric cellulose chains. The three dimensional structures of the catalytic domains of CBHI and CBHII revealed that their active sites are situated in tunnels formed by long loops on the enzymes surface. The active sites of homologous endoglucanases lack these loops and have more open active sites permitting catalytic activity in the internal positions of cellulose chains. Site-directed mutagenesis and structural studies have identified the key catalytic residues of both CBHI and CBHII. Similarly, the primary interaction surface of the cellulose-binding domain has been defined and residues responsible for its tight binding to cellulose identified.

AB - Trichoderma reesei degrades native cellulose utilizing a set of cellulolytic enzymes dominated by two cellobiohydrolases, CBHI and CBHII. These enzymes exhibit the typical two domain architecture of fungal cellulases, and both act primarily as exoglucanases liberating cellobiose from the ends of the polymeric cellulose chains. The three dimensional structures of the catalytic domains of CBHI and CBHII revealed that their active sites are situated in tunnels formed by long loops on the enzymes surface. The active sites of homologous endoglucanases lack these loops and have more open active sites permitting catalytic activity in the internal positions of cellulose chains. Site-directed mutagenesis and structural studies have identified the key catalytic residues of both CBHI and CBHII. Similarly, the primary interaction surface of the cellulose-binding domain has been defined and residues responsible for its tight binding to cellulose identified.

UR - http://www.scopus.com/inward/record.url?scp=0344027838&partnerID=8YFLogxK

U2 - 10.1016/S0921-0423(06)80105-X

DO - 10.1016/S0921-0423(06)80105-X

M3 - Article

VL - 10

SP - 211

EP - 224

JO - Progress in Biotechnology

JF - Progress in Biotechnology

SN - 0921-0423

ER -