ArticleBiochemistry2012
The N-terminus and the chain-length determination domain play a role in the length of the isoprenoid product of the bifunctional Toxoplasma gondii farnesyl diphosphate synthase.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 17 citations in OpenAlex.
- A somatic multiple myeloma mutation unravels a mechanism of oligomerization-mediated product inhibition in GGPPS.The FEBS journal · 2025Article
- Article
- The Property of a Key Amino Acid Determines the Function of Farnesyl Pyrophosphate Synthase inCurrent issues in molecular biology · 2024Article
- Article
- Functional verification and characterization of a type-III geranylgeranyl diphosphate synthase gene fromFrontiers in microbiology · 2022Article
- Structural characterization of geranylgeranyl pyrophosphate synthase GACE1337 from the hyperthermophilic archaeon Geoglobus acetivorans.Extremophiles : life under extreme conditions · 2018Article
- Synergistic Activity between Statins and Bisphosphonates against Acute Experimental Toxoplasmosis.Antimicrobial agents and chemotherapy · 2017Article
- In Vitro and In Vivo Activities of Sulfur-Containing Linear Bisphosphonates against Apicomplexan Parasites.Antimicrobial agents and chemotherapy · 2017Article
- Antiparasitic Activity of Sulfur- and Fluorine-Containing Bisphosphonates against Trypanosomatids and Apicomplexan Parasites.Molecules (Basel, Switzerland) · 2017Article
- New insights into molecular recognition of 1,1-bisphosphonic acids by farnesyl diphosphate synthase.Bioorganic & medicinal chemistry · 2014Article
- Characterization of potential drug targets farnesyl diphosphate synthase and geranylgeranyl diphosphate synthase in Schistosoma mansoni.Antimicrobial agents and chemotherapy · 2013Article
- Cloning and characterization of bifunctional enzyme farnesyl diphosphate/geranylgeranyl diphosphate synthase from Plasmodium falciparum.Malaria journal · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Toxoplasma gondii possesses a bifunctional farnesyl diphosphate (FPP)/geranylgeranyl diphosphate (GGPP) synthase (TgFPPS) that synthesizes C(15) and C(20) isoprenoid diphosphates from isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). This enzyme has a unique arrangement of the fourth and fifth amino acid upstream from the first aspartic rich motif (FARM) where the fourth amino acid is aromatic and the fifth is a cysteine. We mutated these amino acids, converting the enzyme to an absolute FPPS by changing the cysteine to a tyrosine. The enzyme could be converted to an absolute GGPPS by changing both the fourth and fifth amino acids to alanines. We also constructed four mutated TgFPPSs whose regions around the first aspartate rich motif were replaced with the corresponding regions of FPP synthases from Arabidopsis thaliana or Saccharomyces cerevisiae or with the corresponding regions of GGPP synthases from Homo sapiens or S. cerevisiae. We determined that the presence of a cysteine at the fifth position is essential for the TgFPPS bifunctionality. We also found that the length of the N-terminal domain plays a role in determining the specificity and the length of the isoprenoid product. Phylogenetic analysis supports the grouping of this enzyme with other type I FPPSs, but the biochemical data indicate that TgFPPS has unique characteristics that differentiate it from mammalian FPPSs and GGPPSs and is therefore an important drug target.
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