Purification and characterization of an endo-N-acetyl-beta-D-glucosaminidase from the culture medium of Stigmatella aurantiaca DW4.
A novel endo-N-acetyl-beta-D-glucosaminidase (ENGase), acting on the di-N-acetylchitobiosyl part of N-linked glycans, was characterized in the culture medium of Stigmatella aurantiaca DW4. Purified to homogeneity by ammonium sulfate precipitation, gel filtration, and chromatofocusing, this ENGase presents, upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, a molecular mass near 27 kDa. Optimal pH and pI were 4.0 and 6.8, respectively. The enzyme, named ENGase St, exhibits high activity on oligomannoside-type glycoasparagines and glycoproteins and could also hydrolyze hybrid- and complex-type glycoasparagines but does not acts as a murein hydrolase.
Bourgerie
S
S
Institut de Biotechnologie, Université de Limoges, France.
Karamanos
Y
Y
Grard
T
T
Julien
R
R
D001216:Asparagine / Q000031:analogs & derivatives; D002240:Carbohydrate Sequence; D004187:Disaccharides / Q000378:metabolism; D006020:Glycopeptides / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism; D007526:Isoelectric Point; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009231:Myxococcales / Q000201:enzymology* / Q000254:growth & development; D009844:Oligosaccharides / Q000378:metabolism; D013379:Substrate Specificity
D004187:Disaccharides; D006020:Glycopeptides; D006023:Glycoproteins; D009844:Oligosaccharides; C028569:oligomannoside; C010913:N,N-diacetylchitobiose; D001216:Asparagine; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase