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Author Oldfield, Eric ♦ Docampo, Roberto
Source CiteSeerX
Content type Text
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Subject Domain (in DDC) Computer science, information & general works ♦ Data processing & computer science
Subject Keyword Farnesyl Pyrophosphate Synthase ♦ Essential Enzyme ♦ Molecular Mass ♦ Amino Acid ♦ 11-mer Peptide Insertion Present ♦ Drug Development ♦ Nucleotide Sequence ♦ Attrac-tive Target ♦ Several Sequence Motif ♦ Trypanosoma Cruzi Fpps ♦ Several Nitrogen-containing Bisphosphonates ♦ Bone Resorption Therapy ♦ Func-tional Enzyme ♦ Heterologous Ex-pression ♦ Escherichia Coli
Abstract We report the cloning and sequencing of a gene encod-ing the farnesyl pyrophosphate synthase (FPPS) of Trypanosoma brucei. The protein (TbFPPS) is an attrac-tive target for drug development because the growth of T. brucei has been shown to be inhibited by analogs of its substrates, the nitrogen containing bisphosphonates currently in use in bone resorption therapy. The protein predicted from the nucleotide sequence of the gene has 367 amino acids and a molecular mass of 42 kDa. Several sequence motifs found in other FPPSs are present in TbFPPS, including an 11-mer peptide insertion present also in the Trypanosoma cruzi FPPS. Heterologous ex-pression of TbFPPS in Escherichia coli produced a func-tional enzyme that was inhibited by several nitrogen-containing bisphosphonates, such as pamidronate and
Educational Role Student ♦ Teacher
Age Range above 22 year
Educational Use Research
Education Level UG and PG ♦ Career/Technical Study