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Isolated fungal cellulose terminal domains and a synthetic minimum analogue bind to cellulose
Author(s) -
Johansson Gunnar,
Ståhlberg Jerry,
Lindeberg Gunnar,
Engström Åke,
Pettersson Göran
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80168-1
Subject(s) - trichoderma reesei , cellulose , cellulase , chemistry , cleavage (geology) , peptide , biochemistry , enzyme , biology , paleontology , fracture (geology)
The cellulose‐binding properties of the highly conserved terminal region which is common to several fungal cellulases were studied. Domains were prepared by proteolytic cleavage of Trichoderma reesei CBH1 and the corresponding enzyme from Sporotrichum pulverulentum , and a peptide corresponding to residues 462–497 (the C‐terminal part) of Trichoderma CBH1 was synthesized. The three peptides showed similar binding behavior, whereas reduced and S ‐carboxymethylated T. reesei fragment was inactive. This region thus appears to serve as an independent functional domain in which the C‐terminal part is responsible for the binding, which in turn requires an intact three‐dimensional structure.