Purification and characterization of farnesyl pyrophosphate synthase from Capsicum annuum.
Farnesyl 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 89,000 +/- 5000 Da resulting from the association of two apparently identical subunits having a molecular mass of 43,000 +/- 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.
Hugueney
P
P
Laboratoire de Biochemie et Régulations cellulaires UA 568, CNRS, Université Bordeaux I, Talence, France.
Camara
B
B
D002413:Cations, Divalent; D002845:Chromatography; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004122:Dimethylallyltranstransferase / Q000302:isolation & purification* / Q000378:metabolism; D017886:Durapatite; D004591:Electrophoresis, Polyacrylamide Gel; D006882:Hydroxyapatites; D007700:Kinetics; D008970:Molecular Weight; D010944:Plants / Q000201:enzymology*
D002413:Cations, Divalent; D006882:Hydroxyapatites; D017886:Durapatite; D004122:Dimethylallyltranstransferase