Overexpression and characterization of dimeric and tetrameric forms of recombinant serine hydroxymethyltransferase fromBacillus stearothermophilus

@article{Jala2002OverexpressionAC,
  title={Overexpression and characterization of dimeric and tetrameric forms of recombinant serine hydroxymethyltransferase fromBacillus stearothermophilus},
  author={Venkatakrishna R Jala and Vishweshwaraiah Prakash and Narasinga Rao and Handanahal Subbarao Savithri},
  journal={Journal of Biosciences},
  year={2002},
  volume={27},
  pages={233-242}
}
Serine hydroxymethyltransferase (SHMT), a pyridoxal-5′-phosphate (PLP) dependent enzyme catalyzes the interconversion of L-Ser and Gly using tetrahydrofolate as a substrate. The gene encoding for SHMT was amplified by PCR from genomic DNA ofBacillus stearothermophilus and the PCR product was cloned and overexpressed inEscherichia coli. The purified recombinant enzyme was isolated as a mixture of dimer (90%) and tetramer (10%). This is the first report demonstrating the existence of SHMT as a… CONTINUE READING

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