EGIII, a new endoglucanase from Trichoderma reesei: the characterization of both gene and enzyme

Markku Saloheimo; Päivi Lehtovaara; Merja Penttilä; Tuula T. Teeri; J. Ståhlberg; G. Johansson; G. Pettersson; M. Claeyssens; P. Tomme; Jonathan K.C. Knowles

doi:10.1016/0378-1119(88)90541-0

EGIII, a new endoglucanase from Trichoderma reesei: the characterization of both gene and enzyme

Markku Saloheimo, Päivi Lehtovaara, Merja Penttilä, Tuula T. Teeri, J. Ståhlberg, G. Johansson, G. Pettersson, M. Claeyssens, P. Tomme, Jonathan K.C. Knowles

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

273 Citations (Scopus)

Abstract

A novel endoglucanase from Trichoderma reesei, EGIII, has been purified and its catalytic properties have been studied. The gene for that enzyme (egl3) and cDNA have been cloned and sequenced. The deduced EGIII protein shows clear sequence homology to a Schizophyllum commune enzyme (M. Yaguchi, personal communication), but is very different from the three other T. reesei cellulases with known structure. Nevertheless, all the four T. reesei cellulases share two common, adjacent sequence domains, which apparently can be removed by proteolysis. These homologous sequences reside at the N termini of EGIII and the cellobiohydrolase CBHII, but at the C termini of EGI and CBHI. Comparison of the fungal cellulase structures has led to re-evaluation of hypotheses concerning the localization of the active sites.

Original language	English
Pages (from-to)	11-21
Journal	Gene
Volume	63
Issue number	1
DOIs	https://doi.org/10.1016/0378-1119(88)90541-0
Publication status	Published - 15 Mar 1988
MoE publication type	A1 Journal article-refereed

Keywords

active site
cellulase
gene sequence
module shuffling
phage 1 vector
Recombinant DNA
Trichoderma

Access to Document

10.1016/0378-1119(88)90541-0

Cite this

@article{61331ce42f1142a6b1ee8e358a137c1a,

title = "EGIII, a new endoglucanase from Trichoderma reesei: the characterization of both gene and enzyme",

abstract = "A novel endoglucanase from Trichoderma reesei, EGIII, has been purified and its catalytic properties have been studied. The gene for that enzyme (egl3) and cDNA have been cloned and sequenced. The deduced EGIII protein shows clear sequence homology to a Schizophyllum commune enzyme (M. Yaguchi, personal communication), but is very different from the three other T. reesei cellulases with known structure. Nevertheless, all the four T. reesei cellulases share two common, adjacent sequence domains, which apparently can be removed by proteolysis. These homologous sequences reside at the N termini of EGIII and the cellobiohydrolase CBHII, but at the C termini of EGI and CBHI. Comparison of the fungal cellulase structures has led to re-evaluation of hypotheses concerning the localization of the active sites.",

keywords = "active site, cellulase, gene sequence, module shuffling, phage 1 vector, Recombinant DNA, Trichoderma",

author = "Markku Saloheimo and P{\"a}ivi Lehtovaara and Merja Penttil{\"a} and Teeri, {Tuula T.} and J. St{\aa}hlberg and G. Johansson and G. Pettersson and M. Claeyssens and P. Tomme and Knowles, {Jonathan K.C.}",

year = "1988",

month = mar,

day = "15",

doi = "10.1016/0378-1119(88)90541-0",

language = "English",

volume = "63",

pages = "11--21",

journal = "Gene",

issn = "0378-1119",

publisher = "Elsevier",

number = "1",

}

TY - JOUR

T1 - EGIII, a new endoglucanase from Trichoderma reesei

T2 - the characterization of both gene and enzyme

AU - Saloheimo, Markku

AU - Lehtovaara, Päivi

AU - Penttilä, Merja

AU - Teeri, Tuula T.

AU - Ståhlberg, J.

AU - Johansson, G.

AU - Pettersson, G.

AU - Claeyssens, M.

AU - Tomme, P.

AU - Knowles, Jonathan K.C.

PY - 1988/3/15

Y1 - 1988/3/15

N2 - A novel endoglucanase from Trichoderma reesei, EGIII, has been purified and its catalytic properties have been studied. The gene for that enzyme (egl3) and cDNA have been cloned and sequenced. The deduced EGIII protein shows clear sequence homology to a Schizophyllum commune enzyme (M. Yaguchi, personal communication), but is very different from the three other T. reesei cellulases with known structure. Nevertheless, all the four T. reesei cellulases share two common, adjacent sequence domains, which apparently can be removed by proteolysis. These homologous sequences reside at the N termini of EGIII and the cellobiohydrolase CBHII, but at the C termini of EGI and CBHI. Comparison of the fungal cellulase structures has led to re-evaluation of hypotheses concerning the localization of the active sites.

AB - A novel endoglucanase from Trichoderma reesei, EGIII, has been purified and its catalytic properties have been studied. The gene for that enzyme (egl3) and cDNA have been cloned and sequenced. The deduced EGIII protein shows clear sequence homology to a Schizophyllum commune enzyme (M. Yaguchi, personal communication), but is very different from the three other T. reesei cellulases with known structure. Nevertheless, all the four T. reesei cellulases share two common, adjacent sequence domains, which apparently can be removed by proteolysis. These homologous sequences reside at the N termini of EGIII and the cellobiohydrolase CBHII, but at the C termini of EGI and CBHI. Comparison of the fungal cellulase structures has led to re-evaluation of hypotheses concerning the localization of the active sites.

KW - active site

KW - cellulase

KW - gene sequence

KW - module shuffling

KW - phage 1 vector

KW - Recombinant DNA

KW - Trichoderma

UR - http://www.scopus.com/inward/record.url?scp=0023906430&partnerID=8YFLogxK

U2 - 10.1016/0378-1119(88)90541-0

DO - 10.1016/0378-1119(88)90541-0

M3 - Article

C2 - 3384334

AN - SCOPUS:0023906430

SN - 0378-1119

VL - 63

SP - 11

EP - 21

JO - Gene

JF - Gene

IS - 1

ER -

EGIII, a new endoglucanase from Trichoderma reesei: the characterization of both gene and enzyme

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this