Heterologous gene expression and characterization of TK2246, a highly active and thermostable plant type l-asparaginase from Thermococcus kodakarensis.

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ID: 79486
2020
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Abstract
The genome sequence of the hyperthermophilic archaeon Thermococcus kodakarensis contains two putative genes, TK1656 and TK2246, annotated as l-asparaginases. TK1656 has been reported previously. The current report is focused on TK2246, a plant-type l-asparaginase, which consists of 918 nucleotides corresponding to a polypeptide of 306 amino acids. The gene was cloned, expressed in Escherichia coli and the purified gene product was used to determine the properties of the recombinant enzyme. TK2246 was optimally active at 85 °C and pH 7.0 with a specific activity of 767 μmol min mg towards l-asparagine. The enzyme exhibited a 10% activity towards d-asparagine as compared to 100% against l-asparagine. No detectable activity was observed towards l- or d-glutamine. Half-life of the enzyme was nearly 18 h at 85 °C. TK2246 exhibited apparent K and V values of 3.1 mM and 833 μmol min mg, respectively. Activation energy of the reaction, determined from the Arrhenius plot, was 28.3 kJ mol. To the best of our knowledge, this is the first characterization of a plant-type l-asparaginase from class Thermococci of phylum Euryarchaeota.
Reference Key
chohan2020heterologousinternational Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Chohan, Shahid Mahmood;Sajed, Muhammad;Naeem, Sabeel Un;Rashid, Naeem;
Journal International journal of biological macromolecules
Year 2020
DOI
S0141-8130(19)38566-6
URL
Keywords
thermal stability l-asparaginase autocleavage structural stability thermococcus kodakarensis

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