Purification and characterization of farnesyl pyrophosphate synthase from Capsicum annuum

FEBS Letters

Camara, Bilal¹  Hugueney, Philippe¹ 

[1] Laboratoire de Biochimie et Régulations cellulaires U A 568, CNRS, Université Bordeaux I, Avenue des Facultés, 33405 Talence Cedex, France

关键词: Farnesyl pyrophosphate synthase;    Prenyltransferase;    Enzyme purification;    Immunocharacterization;    Capsicum annuum;    DMAPP;    dimethylallyl pyrophosphate;    FPP;    farnesyl pyrophosphate;    GC;    gas chromatography;    GGPP;    geranylgeranyl pyrophosphate;    GPP;    geranyl pyrophosphate;    IPP;    isopentenyl pyrophosphate;    SDS-PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;    TLC;    thin layer chromatography;   

DOI  :  10.1016/0014-5793(90)81093-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Faraesyl pyrophosphate synthase (FPP) displaying dimethylallyl transferase activity (EC 2.5.1.1) and geranyl transferase activity (EC 2.5.1.10) was purified from Capsicum fruits. This prenyltransferase has a molecular mass of 89000 ± 5000 Da resulting from the association of two apparently identical subunits having a molecular mass of 43000 ± 2000 Da. Antibodies raised against Capsicum FPP synthase selectively blocked the transferase activity. Analysis of the immunological relationships between FPP synthase and geranylgeranyl pyrophosphate synthase (EC 2.5.1.1, EC 2.5.1.10 and EC 2.5.1.30) revealed that these two enzymes though performing the same mechanism of catalysis and accepting identical substrates have different antigenic determinants. Thus, in connection to previous work, this immunological study suggests that Capsicum FPP is strictly located in the extraplastidial compartment.

【 授权许可】

Unknown