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The binding of Cellulomonas fimi endoglucanase C (CenC) to cellulose and Sephadex is mediated by the N‐terminal repeats
Author(s) -
Coutinho J. B.,
Gilkes N. R.,
Warren R. A. J.,
Kilburn D. G.,
Miller R. C.
Publication year - 1992
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1992.tb01563.x
Subject(s) - cellulose , cellulase , sephadex , biology , biochemistry , escherichia coli , amino acid , inverted repeat , enzyme , stereochemistry , microbiology and biotechnology , gene , chemistry , genome
Summary Endoglucanase C (CenC) from Celluiomonas fimi binds to cellulose and to Sephadex. The enzyme has two contiguous 150‐amino‐acid repeats (N1 and N2) at its N‐terminus and two unrelated contiguous 100‐amino‐acjd repeats (C1 and C2) at its C‐terminus. Polypeptides corresponding to N1, N1N2, C1, and C1C2 were produced by expression of appropriate cenC gene fragments in Escherichia coli. N1N2, but not N1 alone, binds to Sephadex; both polypeptides bind to Avicel, (a heterogeneous cellulose preparation containing both crystalline and non‐crystalline components). Neither C1 nor C1C2 binds to Avicel or Sephadex. N1N2 and N1 bind to regenerated (amorphous') cellulose but not to bacterial crystalline cellulose; the cellulose‐binding domain of C. fimi exoglucanase Cex binds to both of these forms of cellulose. Amino acid sequence comparison reveals that N1 and N2 are distantly related to the cellulose‐binding domains of Cex and C. fimi endoglucanases A and B.