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Literature summary extracted from

  • Lin, F.; Liu, C.; Liu, Y.; Zhang, Y.; Wang, K.; Jeng, W.; Ko, T.; Cao, R.; Wang, A.; Oldfield, E.
    Mechanism of action and inhibition of dehydrosqualene synthase (2010), Proc. Natl. Acad. Sci. USA, 107, 21337-21342.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.96 in with its reaction intermediate, presqualene diphosphate, the dehydrosqualene product, as well as a series of inhibitors. The results indicate that, on initial diphosphate loss, the primary carbocation so formed bends down into the interior of the protein to react with C2,3 double bond in the prenyl acceptor to form presqualene diphosphate, with the lower two-thirds of both presqualene diphosphate chains occupying essentially the same positions as found in the two farnesyl chains in the substrates. The second-half reaction is then initiated by the presqualene diphosphate returning back to the Mg2+ cluster for ionization, with the resultant dehydrosqualene so formed being trapped in a surface pocket Staphylococcus aureus

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.96 Y129A no activity with substrate farnesyl diphophate, 7% residual activity with geranyl diphosphate Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.96 Staphylococcus aureus A9JQL9
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Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.96 2 (2E,6E)-farnesyl diphosphate = 15-cis-4,4'-diapophytoene + 2 diphosphate prenyl diphosphate binding site S1 farnesyl diphosphate ionizes to form the 1'-carbocation. This carbocation moves down into the interior of the protein to react with C2,3 in the prenyl diphosphate binding site S2 farnesyl diphosphate. The second PPi then moves up into the S1 site to interact with the three Mg2+, and the cyclopropylcarbinyl cation so formed then rearranges, forming dehydrosqualene binds to the surface pocket Staphylococcus aureus