Comparative specificity of geranylgeranyl pyrophosphate synthetase of Micrococcus lysodeikticus and pumpkin

J Biochem. 1975 Dec;78(6):1177-81. doi: 10.1093/oxfordjournals.jbchem.a131014.

Abstract

Comparative studies on the substrate specificity of geranylgeranyl pyrophosphate synthetase from Micrococcus lysodeikticus and from pumpkin seedlin revealed that geranyl pyrophosphate was the most active of the natural substrates for the pumpkin enzyme, whereas it was the least active for the bacterial enzyme. A marked difference was also observed between the enzymes from these two sources as regards the reactivity of 3-methyl-2-alkenyl pyrophosphates as a function of the size of the alkyl group.

Publication types

  • Comparative Study

MeSH terms

  • Kinetics
  • Micrococcus / enzymology*
  • Phosphoric Acids
  • Plants / enzymology*
  • Species Specificity
  • Structure-Activity Relationship
  • Terpenes
  • Transferases / metabolism*

Substances

  • Phosphoric Acids
  • Terpenes
  • Transferases