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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Recombinant squalene synthase. Synthesis of non-head-to-tail isoprenoids in the absence of NADPH.

Squalene synthase (SQase) catalyzes two consecutive reactions in sterol biosynthesis. The first is the condensation of two molecules of farnesyl diphosphate ( FPP) to form a cyclopropylcarbinyl intermediate, presqualene diphosphate ( PSPP). The subsequent conversion of PSPP to squalene (SQ) involves an extensive rearrangement of the carbon skeleton and a NADPH-dependent reduction. Incubation of a truncated soluble form of recombinant yeast SQase with FPP in buffer lacking NADPH gave (1R,2R,3R)-PSPP. As the incubation continued, SQase catalyzed the subsequent conversion of PSPP to a mixture of triterpenes. Two of the major products, (Z)-dehydrosqualene (DSQ) and (R)-12-hydroxysqualene (HSQ), have the same 1'-1 linkage between the farnesyl units from FPP that is found in squalene. The other major product, (10S,13S)-10-hydroxybotryococcene (HBO), has a 1'-3 linkage between the farnesyl units. Small quantities of (S)-HSQ and (10R,13S)-HBO were also formed. Three additional triterpenes, the allylic isomers of HSQ and HBO, and an unidentified alcohol were produced in minor amounts. A methyl ether corresponding to HSQ was detected when methanol was present in the incubation buffer. These compounds are the expected "solvolysis" products from PSPP. They provide strong support for mechanisms that propose cyclopropylcarbinyl cations as intermediates in the SQase-catalyzed rearrangement of PSPP to SQ and unambiguously demonstrate that the catalytic machinery of SQase is capable of synthesizing a variety of irregular isoprenoids.[1]


  1. Recombinant squalene synthase. Synthesis of non-head-to-tail isoprenoids in the absence of NADPH. Jarstfer, M.B., Zhang, D.L., Poulter, C.D. J. Am. Chem. Soc. (2002) [Pubmed]
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