Structural prediction,cloning,expression and enzymatic propertity of aromatic amino acid transaminase from Enterobacter tabaci
XU Ruimin
SHAO Hua
LI Chenfei
SHAN Mingming
WEI Tao
Abstract:To enhance the potential application of aromatic amino acid transaminase(AAT)in the synthesis of auxin(IAA)and promotion of crop growth,bioinformatics methods were applied to analyze and predict the structure of AAT from Enterobacter tabaci strain β7.Then,this AAT was cloned,expressed and purified in Escherichia coli,and the enzymatic properties of recombinant AAT were determined.The bioinformatics analysis results revealed that the length of this AAT protein is composed of 396 amino acids.The key residue in the active center of this AAT was Lys246.The molecular weight of the recombinant AAT expressed in E.coli was approximately 43 kDa.The optimal substrate for recombinant AAT was tryptophan,at a temperature of 50℃and a pH value of 8.0.Cu2+had a certain activating effect on enzyme activity,and recombinant AAT showed good tolerance to the organic solvent ethanol.These results provided a theoretical basis for the AAT enzyme modification and the construction of high-yield auxin engineering bacteria.
Keywords:Enterobacter tabaciaromatic amino acid transaminaseauxinstructural predictioncloning and expressionenzymatic property
Publication Date:2025-04-15
Online Publishing Date:2025-08-15(First online date of this platform, not the publication date of the document)
Pages:8( 100-107 )
Journal of Light Industry

Journal of Light Industry

PKU
ISSN:2096-1553
Year, Vol.(Issue):2025,40(2)