Glycosylation of bacterial cellulases prevents proteolytic cleavage between functional domains

FEBS Letters

Singh, B.²  Miller, R.C.¹  Moser, B.¹  Gilkes, N.R.¹  Kilburn, D.G.¹  Langsford, M.L.¹  Warren, R.A.J.¹ 

[1] Department of Microbiology, University of British Columbia, Vancouver, British Columbia V6T 1W5, Canada;Department of Immunology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

关键词: Cellulase;    Proteolysis;    Domain;    Glycosylation;    (Cellulomonas);    EngA;    endoglucanase A;    Exg;    exoglucanase;    CMC;    carboxymethylcellulose;    HBAH;    hydroxybenzoic acid hydrazide reagent;    PMSF;    phenylmethylsulfonyl fluoride;    pNPC;    p-nitrophenyl-β-D-cellobioside;   

DOI  :  10.1016/0014-5793(87)81150-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Glycosylated cellulases from Cellulomonas fimi were compared with their non-glycosylated counterparts synthesized in Escherichia coli from recombinant DNA. Glycosylation of the enzymes does not significantly affect their kinetic properties, or their stabilities towards heat and pH. However, the glycosylated enzymes are protected from attack by a C. fimi protease when bound to cellulose, while the non-glycosylated enzymes yield active, truncated products with greatly reduced affinity for cellulose.

【 授权许可】

Unknown