JOURNAL OF LIGHT INDUSTRY

CN 41-1437/TS  ISSN 2096-1553

Volume 40 Issue 2
April 2025
Article Contents
XU Ruimin, SHAO Hua, LI Chenfei, et al. Structural prediction, cloning, expression and enzymatic propertity of aromatic amino acid transaminase from Enterobacter tabaci[J]. Journal of Light Industry, 2025, 40(2): 100-107. doi: 10.12187/2025.02.011
Citation: XU Ruimin, SHAO Hua, LI Chenfei, et al. Structural prediction, cloning, expression and enzymatic propertity of aromatic amino acid transaminase from Enterobacter tabaci[J]. Journal of Light Industry, 2025, 40(2): 100-107. doi: 10.12187/2025.02.011 shu

Structural prediction, cloning, expression and enzymatic propertity of aromatic amino acid transaminase from Enterobacter tabaci

  • Corresponding author: WEI Tao, weit8008@zzuli.edu.cn
  • Received Date: 2024-03-07
    Accepted Date: 2024-04-18
  • 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.
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