N-glycosylation is necessary for enzymatic activity of a beetle (Apriona germari) cellulase.

doi:10.1016/j.bbrc.2005.01.131

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Article

N-glycosylation is necessary for enzymatic activity of a beetle (Apriona germari) cellulase.

Biochemical and biophysical research communications - 1 Apr 2005

Wei Ya Dong, Lee Seong Jin, Lee Kwang Sik, Gui Zhong Zheng, Yoon Hyung Joo, Kim Iksoo, Je Yeon Ho, Guo Xijie, Sohn Hung Dae, Jin Byung Rae

Abstract excerpt

We previously reported that the beta-1,4-endoglucanase (EGase) belonging to glycoside hydrolase family 45 cloned from the mulberry longicorn beetle, Apriona germari (Ag-EGase I), is composed of 237 amino acid residues and has a potential N-glycosylation site at 97-100 amino acid residues (NSTF). We here describe the N-glycosylation and its role for enzymatic activity of the Ag-EGase I. The N-glycosylation of...

Topics

Animals
Base Sequence
Binding Sites
Blotting, Western
Carbohydrates
Cell Line
Cellulase
Cloning, Molecular
Coleoptera
Electrophoresis, Polyacrylamide Gel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Glycosylation

Insecta

Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase

Models, Genetic

Molecular Sequence Data

Mutagenesis, Site-Directed

Mutation

Protein Structure, Tertiary

Source

Open in PubMed

Identifiers

PMID: 15721311
DOI: 10.1016/j.bbrc.2005.01.131

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