Characterization of DAHP Synthase L183Q Mutation Comparison to Wild One by Prokaryotic Expression System

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/).

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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  -