AI Article Synopsis
- Chain elongation prenyltransferases are enzymes that help build isoprenoids by adding hydrocarbon groups to isopentenyl diphosphate (IPP).
- Researchers synthesized several bis-substrate analogues, including 3-OPP/OPP, 4-OPP/OPP, 5-OPP/OPP, and their thiol counterparts.
- Some of these analogues, particularly 4-OPP/OPP and 5-OPP/OPP, were found to be strong inhibitors of avian farnesyl diphosphate synthase, with specific inhibition constants (KI) indicating their effectiveness.
Article Abstract
Chain elongation prenyltransferases catalyze the addition of the hydrocarbon moiety of allylic isoprenoid diphosphates to the carbon-carbon double bond in isopentenyl diphosphate (IPP) in the primary building reactions in the isoprenoid biosynthetic pathway. Bis-O-diphosphate analogues 3-OPP/OPP, 4-OPP/OPP, and 5-OPP/OPP and bis-thiolodiphosphate bisubstrate analogues 3-SPP/SPP, 4-SPP/SPP, and 5-SPP/SPP were synthesized. The analogues 4-OPP/OPP, 5-OPP/OPP, 4-SPP/SPP, and 5-SPP/SPP were excellent competitive inhibitors of avian farnesyl diphosphate synthase with KI = 1.0 ± 0.12 μM, KI = 0.5 ± 0.2 μM, KI = 0.7 ± 0.3 μM, and KI = 2.9 ± 0.27 μM, respectively, whereas, analogues 3-OPP/OPP and 3-SPP/SPP displayed mixed type inhibition with KI = 1.4 μM and KI = 5.5 μM, respectively.
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| http://dx.doi.org/10.1021/acs.joc.6b00664 | DOI Listing |
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