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pubmed:abstractText |
Citronellyl- and geranylphosphonic acids and the corresponding phosphonylphosphates were made and tested as inhibitors of liver prenyltransferase. Kinetic analysis showed that citronellyl- and geranylphosphonylphosphate were powerful inhibitors of the enzyme, and that they were competitive inhibitors with geranyl diphosphate and noncompetitive inhibitors with isopentenyl diphosphate. Two inhibition constants, representing the equilibria [E][I]/[EI] = K5 and [ES1][I]/[ES1I] = K9, have been defined for the inhibitors. For citronellylphosphonylphosphate, the value of K5 was 1.25 microM and K9 was 3.30 microM; for geranylphosphonylphosphate, K5 = 1.50 microM and K9 = 1.60 microM. The phosphonates were very poor linear mixed noncompetitive inhibitors with respect to both substrates of the transferase.
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