
Technique(s) used for Glycosylation Detection | Mass shift detected after deglycosylation with Endo Hf and PNGase F |
Technique(s) used for Glycosylated Residue(s) Detection | N-terminal sequencing |
Protein Glycosylation- Implication | There is a large influence of N glycosylation on the thermostability of the hybrid enzyme. 16- and 133-fold decrease of thermostability has been observed after treatment with endoglycosidase H and peptide:N-glycosidase F (that remove glycans). This indicates that N-glycans are a major determinant for the resistance of this hybrid glucanase to thermal inactivation. |
Glycan Information |
Glycan Annotation | Linkage: GlcNAc-N-Asn |
Literature |
Year of Identification | 1994 |
Year of Identification Month Wise | 1994.01.01 |
Year of Validation | 1994 |
Reference | Hahn, M., Keitel, T. and Heinemann, U., 1995. Crystal and Molecular Structure at 0.16‐nm Resolution of the Hybrid Bacillus Endo‐1, 3‐1, 4‐β‐D‐Glucan 4‐Glucanohydrolase H (A16‐M). European journal of biochemistry, 232(3), pp.849-858. |
Contact | Research group crystallography, Max Delbrück Center for Molecular Medicine, Berlin, Germany. |
Reference | Meldgaard, M., 1994. Different effects of N-glycosylation on the thermostability of highly homologous bacterial (1, 3-1, 4)-β-glucanases secreted from yeast. Microbiology, 140(1), pp.159-166. |
Corresponding Author | M Meldgaard |
Contact | Department of Physiology, Carlsberg Laboratory, Copenhagen, Denmark. |
Reference | Hahn, M., Piotukh, K., Borriss, R. and Heinemann, U., 1994. Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis. Proceedings of the National Academy of Sciences, 91(22), pp.10417-10421. |
Contact | Research group crystallography, Max Delbrück Center for Molecular Medicine, Berlin, Germany. |
Reference | Keitel, T., Meldgaard, M. and Heinemann, U., 1994. Cation binding to a Bacillus (1, 3–1, 4)‐β‐glucanase Geometry, affinity and effect on protein stability. European Journal of Biochemistry, 222(1), pp.203-214. |
Corresponding Author | Udo Heinemann |
Contact | Institute of Crystallography, Freie Universität Berlin, Germany |
Reference | Olsen, O. and Thomsen, K.K., 1991. Improvement of bacterial β-glucanase thermostability by glycosylation. Microbiology, 137(3), pp.579-585. |
Corresponding Author | Karl Kristian Thomsen |
Contact | Carlsberg Laboratory, Department of Physiology, Gamle Carlsbergvej 10, DK-2500 Copenhagen Valby, Denmark |
Reference | Hahn, M., Keitel, T. and Heinemann, U. (1995) Crystal and molecular structure at 0.16-nm resolution of the hybrid Bacillus endo-1,3-1,4-beta-D-glucan 4-glucanohydrolase H(A16-M). Eur J Biochem, 232, 849-858. [PubMed: 7588726] |
Author | Hahn, M., Keitel, T. and Heinemann, U. |
Research Group | Research Group on Crystallography, Max Delbrück Center for Molecular Medicine, Berlin, Germany. |
Corresponding Author | Heinemann, U |
Contact | Research Group on Crystallography, Max Delbrück Center for Molecular Medicine, Berlin, Germany. |
Reference | Meldgaard, M. and Svendsen, I. (1994) Different effects of N-glycosylation on the thermostability of highly homologous bacterial (1,3-1,4)-beta-glucanases secreted from yeast. Microbiology, 140 ( Pt 1), 159-166. [PubMed: 8162185] |
Author | Meldgaard, M. Svendsen, I. |
Research Group | Department of Physiology, Carlsberg Laboratory, Copenhagen, Denmark. |
Corresponding Author | Svendsen, I. |
Contact | Department of Physiology, Carlsberg Laboratory, Copenhagen, Denmark. |
Reference | Hahn, M., Piotukh, K., Borriss, R. and Heinemann, U. (1994) Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis. Proc Natl Acad Sci U S A, 91, 10417-10421. [PubMed: 7937966] |
Author | Hahn, M., Piotukh, K., Borriss, R. Heinemann, U. |
Research Group | Max-Delbrück-Center for Molecular Medicine, Berlin, Germany. |
Corresponding Author | Heinemann, U. |
Contact | Max-Delbrück-Center for Molecular Medicine, Berlin, Germany. |
Reference | Keitel, T., Meldgaard, M. and Heinemann, U. (1994) Cation binding to a Bacillus (1,3-1,4)-beta-glucanase. Geometry, affinity and effect on protein stability. Eur J Biochem, 222, 203-214. [PubMed: 8200344] |
Author | Keitel, T., Meldgaard, M. Heinemann, U. |
Research Group | Institute of Crystallography, Freie Universität Berlin, Germany |
Corresponding Author | Heinemann, U. |
Contact | Institute of Crystallography, Freie Universität Berlin, Germany |
Reference | Olsen, O., Thomesen, K. K. (1991) Improvement of bacterial P-glucanase thermostability by glycosylation. J Gen Microbiol, 137, 579–585. |
Author | Olsen, O., Thomesen, K. K. |
Research Group | Carlsberg Laboratory, Department of Physiology, Gamle Carlsbergvej 10, DK-2500 Copenhagen Valby, Denmark |
Corresponding Author | Thomesen, K. K. |
Contact | Carlsberg Laboratory, Department of Physiology, Gamle Carlsbergvej 10, DK-2500 Copenhagen Valby, Denmark |