The overall objectives of this project are to purify the Lactobacillus plantarum enzymes undecaprenyl pyrophosphate synthetase and undecaprenol phosphokinase to homogeneity and characterize them with respect to their substrate specificity, phospholipid or membrane requirements and the stereochemical structure of their substrates and products. Specific areas of emphasis will be (1) continued application of chromatographic and electrophoretic methods to purify both the synthetase and phosphokinase, (2) determination of synthetase specificity for stereochemically pure C15 and C20 allylic pyrophosphates using double label experiments and chromatographic characterization of the products, (3) chemical synthesis of isopentenyl pyrophosphate analogues and testing their suitability as substrates, and (4) purification and characterization of the membrane associated undecaprenol phosphokinase. BIBLIOGRAPHIC REFERENCES: Allen, C.M., Jr., Keenan, M.V, and Sack, J. Arch. Biochem. Biophys. 175, 235 (1976). Lactobacillus plantarum Undecaprenyl Pyrophosphate Synthetase: Purification and Reaction Requirements (previously reported as acceptable with appropriate revision). Allen, C.M., Jr. and Muth, J.D. Federation Proceedings 36, 852 (1977). Lipid Activation of Undecaprenyl Pyrophosphate Synthetase from Lactobacillus plantarum.
NIH ExPorter
NIH ExPorter