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Quantitative and Qualitative Method for Sphingomyelin by LC-MS Using Two Stable Isotopically Labeled Sphingomyelin Species
Published on: May 7, 2018
Molecular and biochemical characterization of squalene synthase from Siraitia grosvenorii
Heling Su1, Yongming Liu2, Yalun Xiao2
1Department of Biochemistry and Molecular Biology, Guangxi Medical University, Nanning, Guangxi, 530000, China.
Objectives:
To clone and characterize the squalene synthase from Siraitia grosvenorii (SgSQS).
Results:
The gene encoding SgSQS was cloned. SgSQS has 417 amino acid residues with an pI of 7.3. There are 32 phosphorylation sites in its sequence: S48 as well as S196 play important roles in regulation of enzyme activity. The enzyme is a monomeric protein with a cave-like active center formed by α helixes and has two transmembrane domains at its C-terminus. SgSQS mRNA expression in stem and root were about twice as much as that in leaf and peel. Full-length SgSQS with measurable catalytic activity was expressed in Escherichia coli. SgSQS activity was optimal at 37 °C and pH 7.5 respectively.
Conclusion:
SgSQS gene was cloned, and the molecular structure and biochemical function of SgSQS were characterized.
