N-Glycosylation Sited at Residues of Catalytic Center Could Repress The Activity of Endoglucanase from Rhizopus Stolonifer
- https://doi.org/10.2991/bep-16.2017.25How to use a DOI?
- N-glycosylation; endoglucanase; molecular dynamics simulation; Rhizopus stolonifer
As a common post-translational modification of proteins, glycosylation has been proven effectively influence the activity of enzyme. To improve the activity of endoglucanase (EGII) from Rhizopus stolonifer TP-02, we studied the effect of glycosylation on the structure and activity of EGII. Two potential glycosylation sites (N84 and N150) were predicted, of which N150 was located in the entrance of catalytic domain (CD). N84D and N150D was obtained by overlapping PCR and expressed in Pichia pastoris for purification. Compared with EGII, the specific activity of N84D was decreased by 28.7%, whereas the activity of N150D was increased by 56.9%. Dynamics simulations results indicated that the N-glycans located in the active center could repress the activity of EGII due to the steric hindrances that effectively hinder the cellulose chains to enter the CD domain.
- © 2017, the Authors. Published by Atlantis Press.
- Open Access
- This is an open access article distributed under the CC BY-NC license (http://creativecommons.org/licenses/by-nc/4.0/).
Cite this article
TY - CONF AU - Bin TANG AU - Yingying ZHANG AU - Wei CHENG AU - Qingqing ZHANG AU - Song LI PY - 2016/12 DA - 2016/12 TI - N-Glycosylation Sited at Residues of Catalytic Center Could Repress The Activity of Endoglucanase from Rhizopus Stolonifer BT - Proceedings of the 2016 International Conference on Biological Engineering and Pharmacy (BEP 2016) PB - Atlantis Press SP - 118 EP - 123 SN - 2468-5747 UR - https://doi.org/10.2991/bep-16.2017.25 DO - https://doi.org/10.2991/bep-16.2017.25 ID - TANG2016/12 ER -