Isolation and characterization of farnesyl diphosphate synthase from the cotton boll weevil, Anthonomus grandis
作者： A. Huma Taban , Claus Tittiger , Gary J. Blomquist , William H. Welch
DOI: 10.1002/ARCH.20302
关键词:
摘要: Farnesyl diphosphate synthase (FPPS) catalyzes the consecutive condensation of two molecules isopentenyl with dimethylallyl to form farnesyl (FPP). In insects, FPP is used for synthesis ubiquinones, dolicols, protein prenyl groups, and juvenile hormone. A full-length cDNA FPPS was cloned from cotton boll weevil, Anthonomus grandis (AgFPPS). AgFPPS consists 1,835 nucleotides encodes a 438 amino acids. The deduced acid sequence has high similarity previously isolated insect FPPSs other known FPPSs. Recombinant expressed in E. coli converted labeled presence FPP. Southern blot analysis indicated single copy gene. Using molecular modeling, three-dimensional structure coleopteran determined compared X-ray crystal avian FPPS. α-helical fold conserved size active site cavity consistent enzyme being © 2009 Wiley Periodicals, Inc.
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