摘要
Cellulases are important glycosyl hydrolases （GHs） that hydrolyze cellulose polymers into smaller oligosaccharides by breaking the cellulose β （1→4） bonds, and they are widely used to produce cellulosic ethanol from the plant biomass. N-linked and O-linked glycosylations were proposed to impact the catalytic efficiency, cellulose binding affinity and the stability of cellulases based on observations of individual cellulases. As far as we know, there has not been any systematic analysis of the distributions of N-linked and O-linked glycosylated residues in cellulases, mainly due to the limited annotations of the relevant functional domains and the glycosylated residues. We have computationally annotated the functional domains and glycosylated residues in cellulases, and conducted a systematic analysis of the distributions of the N-linked and O-linked glycosylated residues in these enzymes. Many N-linked glycosylated residues were known to be in the GH domains of cellulases, but they are there probably just by chance, since the GH domain usually occupies more than half of the sequence length of a cellulase. Our analysis indicates that the O-linked glycosylated residues are significantly enriched in the linker re- gions between the carbohydrate binding module （CBM） domains and GH domains of cellulases. Possible mechanisms are discussed.
Cellulases are important glycosyl hydrolases （GHs） that hydrolyze cellulose polymers into smaller oligosaccharides by breaking the cellulose β （1→4） bonds, and they are widely used to produce cellulosic ethanol from the plant biomass. N-linked and O-linked glycosylations were proposed to impact the catalytic efficiency, cellulose binding affinity and the stability of cellulases based on observations of individual cellulases. As far as we know, there has not been any systematic analysis of the distributions of N-linked and O-linked glycosylated residues in cellulases, mainly due to the limited annotations of the relevant functional domains and the glycosylated residues. We have computationally annotated the functional domains and glycosylated residues in cellulases, and conducted a systematic analysis of the distributions of the N-linked and O-linked glycosylated residues in these enzymes. Many N-linked glycosylated residues were known to be in the GH domains of cellulases, but they are there probably just by chance, since the GH domain usually occupies more than half of the sequence length of a cellulase. Our analysis indicates that the O-linked glycosylated residues are significantly enriched in the linker re- gions between the carbohydrate binding module （CBM） domains and GH domains of cellulases. Possible mechanisms are discussed.
基金
supported in part by the National Science Foundation of USA (Grants DBI-0354771,ITR-IIS-0407204,DBI-0542119 and CCF0621700),the grant for the BioEnergy Science Center,and a Distinguished Scholargrant from the Georgia Cancer Coalition
