Characterization of DAHP Synthase L183Q Mutation Comparison to Wild One by Prokaryotic Expression System
Authors
Hansong Yu, Tian Hao, Yuhua Wang, Chunhong Piao, Junmei Liu, Yaohui Hu
Corresponding Author
Hansong Yu
Available Online June 2015.
- DOI
- 10.2991/ap3er-15.2015.72How to use a DOI?
- Keywords
- DAHP synthase; Catalytic properties; Recombinant key enzyme of amino acid synthesize
- Abstract
The prokaryotic expression system was employed in order to compare the catalytic properties of L183Q mutation and wild DAHP synthase enzyme. The gene of L183Q mutation and wild DAHP synthase enzyme was cloned and expressed by pET vector system and Eco.li BL21. The specific activity of the two recombinant enzyme was determinated. The result show that the relative activity of wild and L183Q mutation is 2.4u/mg and 3.6u/mg, respectively. But the optimal pH and temperature difference between wild and mutation DAHP synthase enzyme is not significant (p>0.05).
- Copyright
- © 2015, 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 - Hansong Yu AU - Tian Hao AU - Yuhua Wang AU - Chunhong Piao AU - Junmei Liu AU - Yaohui Hu PY - 2015/06 DA - 2015/06 TI - Characterization of DAHP Synthase L183Q Mutation Comparison to Wild One by Prokaryotic Expression System BT - Proceedings of the 2015 Asia-Pacific Energy Equipment Engineering Research Conference PB - Atlantis Press SP - 306 EP - 309 SN - 2352-5401 UR - https://doi.org/10.2991/ap3er-15.2015.72 DO - 10.2991/ap3er-15.2015.72 ID - Yu2015/06 ER -