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Published on: October 25, 2024
Characterization of a squalene synthase from the thraustochytrid microalga Aurantiochytrium sp. KRS101
Won-Kyung Hong1, Sun-Yeon Heo, Hye-Mi Park
1Applied Microbiology Research Center, Bio-Materials Research Institute, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Jeonbuk 580-185, Korea.
Abstract:
The gene encoding squalene synthase (SQS) of the lipidproducing heterotrophic microalga Aurantiochytrium sp. KRS101 was cloned and characterized. The krsSQS gene is 1,551 bp in length and has two exons and one intron. The open reading frame of the gene is 1,164 bp in length, yielding a polypeptide of 387 predicted amino acid residues with a molecular mass of 42.7 kDa. The deduced krsSQS sequence shares at least four conserved regions known to be required for SQS enzymatic activity in other species. The protein, tagged with His6, was expressed into soluble form in Escherichia coli. The purified protein catalyzed the conversion of farnesyl diphosphate to squalene in the presence of NADPH and Mg(2+). This is the first report on the characterization of an SQS from a Thraustochytrid microalga.
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