In silico modeling and analysis of squalene synthase-like 1 (SSL-1) enzyme from green microalga Botryococcus terribilis AICB 872
DOI:
https://doi.org/10.24193/subbbiol.2020.1.01Keywords:
Botryococcus terribilis, squalene synthase-like 1, 3D structure prediction, AICB strain, biofuel.Abstract
The genus Botryococcus contains a small number of green, colonial algae, with some taxa still uncertain. B. braunii is the most extensively studied species of the genus because of its hydrocarbon oils which can be used as an alternative energy source. Some B. terribilis AICB strains were previously described showing their ability to synthesize C30–C32 botryococcenes similar to those produced by chemical race B of B. braunii strains. The present study aimed to investigate the structural features of SSL-1 enzyme involved in the biosynthesis of presqualene diphosphate from B. terribilis AICB 872, and its functional conservation by means of computational proteomics and molecular biology techniques. Using PCR amplification we obtained a 3811bp contig containing the sequence of SSL-1 gene. The homology modeling analysis revealed the presence of alpha helical structures and a small beta sheet which are forming the SSL-1 catalytic core. Coil structures and both N and C terminus regions of the protein are characterized by highly disordered structural fragments. Finally, our data integrated within the available information in the literature allowed us to presume that the formation of presqualene diphosphate, the first step of hydrocarbon biosynthesis in B. terribilis strain occurs in a similar fashion with that described in B. braunii.
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