Glycosylation of bacterial cellulases prevents proteolytic cleavage between functional domains.
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.
D000192:Actinomycetales / Q000201:enzymology*; D002384:Catalysis; D002480:Cellulase / Q000235:genetics / Q000378:metabolism*; D002482:Cellulose / Q000378:metabolism; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D006031:Glycosylation; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007118:Immunoassay; D007700:Kinetics; D010446:Peptide Fragments / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D012697:Serine Endopeptidases / Q000378:metabolism
D010446:Peptide Fragments; D011994:Recombinant Proteins; D002482:Cellulose; D002480:Cellulase; D012697:Serine Endopeptidases