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Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei
Uppsala University.
Uppsala University.
Uppsala University.
Uppsala University.
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1996 (English)In: JOURNAL OF MOLECULAR BIOLOGY, ISSN 0022-2836, Vol. 264, no 2, 337-349 p.Article in journal (Other scientific) Published
Abstract [en]

The roles of the residues in the catalytic trio Glu212-Asp214-Glu217 in cellobiohydrolase I (CBHI) from Trichoderma reesei have been investigated by changing these residues to their isosteric amide counterparts. Three mutants, E212Q, D214N and E217Q, were

Place, publisher, year, edition, pages
ACADEMIC PRESS LTD , 1996. Vol. 264, no 2, 337-349 p.
Keyword [en]
cellulase; cellobiohydrolase I; catalytic activity; active-site mutant; crystal structure; SITE-DIRECTED MUTAGENESIS; ACID-SEQUENCE SIMILARITIES; FREE R-VALUE; GLYCOSYL HYDROLASES; ENDOGLUCANASE-I; MACROMOLECULAR STRUCTURES; 3-DIMENSIONAL STRUCTURE; CELLU
Identifiers
URN: urn:nbn:se:uu:diva-79794OAI: oai:DiVA.org:uu-79794DiVA: diva2:107707
Note
Addresses: UNIV UPPSALA, CTR BIOMED, DEPT BIOL MOL, S-75124 UPPSALA, SWEDEN. VTT BIOTECHNOL & FOOD RES, FIN-02044 ESPOO, FINLAND. STATE UNIV GHENT, FAC SCI, DEPT BIOCHEM MICROBIOL & PHYSIOL, B-9000 GHENT, BELGIUM.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-15

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