In Silico study of the conformational flexibility of point mutated Geobacillus stearothermophilus farnesyl diphosphate synthase

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Abstract

Farnesyl diphosphate synthase from Geobacillus stearothermophilus (GsFPPS) is a thermophilic enzyme which belongs to the prenyltransferase family. We found that the point mutation of an amino acid located on the fifth position upstream of the first aspartate-rich motif (FARM) in GsFPPS (tyr81) affects its flexibility and activity. Enzymatic activities of wild-type GsFPPS, Y81D, Y81R, and Y81S were measured by a 14C radioactivity assay. Their flexibilities were assessed by monitoring the fluorescence intensity changes due to the presence of a collisional quencher and also by coarse-grained molecular dynamics (MD) simulations. Y81R and Y81S showed enhanced activities of up to 1.7-fold, while activity of Y81D was reduced by 1.2-fold. The differences in activity between these enzyme variants are caused by the differences in conformational flexibility, especially in terms of the dynamics of the areas near the active site.

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  • CRID
    1390845713036595328
  • NII Article ID
    130007599094
  • DOI
    10.11425/sst.7.109
  • ISSN
    21871590
    21864942
  • NDL BIB ID
    029482990
  • Text Lang
    ja
  • Data Source
    • JaLC
    • NDL
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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