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THE CELLULOSE-BINDING DOMAIN OF ENDOGLUCANASE-A (CENA) FROM CELLULOMONAS-FIMI - EVIDENCE FOR THE INVOLVEMENT OF TRYPTOPHAN RESIDUES IN BINDING

TitleTHE CELLULOSE-BINDING DOMAIN OF ENDOGLUCANASE-A (CENA) FROM CELLULOMONAS-FIMI - EVIDENCE FOR THE INVOLVEMENT OF TRYPTOPHAN RESIDUES IN BINDING
Publication TypeJournal Article
Year of Publication1994
AuthorsDin, N, Forsythe, IJ, Burtnick, LD, Gilkes, NR, Miller, RC, Warren, RAJ, Kilburn, DG
JournalMolecular Microbiology
Volume11
Pagination747-755
Date PublishedFeb
Type of ArticleArticle
ISBN Number0950-382X
KeywordsBACTERIAL CELLULASE, CELLOBIOHYDROLASES, CLONING, DNA, FLUORESCENS SUBSP CELLULOSA, FUNCTIONAL DOMAINS, GENE, PROTEIN, SEQUENCE, THERMOMONOSPORA-FUSCA
Abstract

Cellulomonas fimi endo-beta-1-4-glucanase A (CenA) contains a discrete N-terminal cellulose-binding domain (CBDCenA). Related CBDs occur in at least 16 bacterial glycanases and are characterized by four highly conserved Trp residues, two of which correspond to W14 and W68 of CBDCenA. The adsorption of CBDCenA to crystalline cellulose was compared with that of two Trp mutants (W14A and W68A). The affinities of the mutant CBDs for cellulose were reduced by approximately 50- and 30-fold, respectively, relative to the wild type. Physical measurements indicated that the mutant CBDs fold normally. Fluorescence data indicated that W14 and W68 were exposed on the CBD, consistent with their participation in binding to cellobiosyl residues on the cellulose surface.

URL<Go to ISI>://A1994MW53600013