Pig liver phosphomevalonate kinase: Kinetic mechanism

Jaime Eyzaguirre, David Valdebenito, Emilio Cardemil

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

Phosphomevalonate kinase catalyzes the phosphorylation of phosphomevalonate to diphosphomevalonate by ATP, one of the initial steps in the biosynthesis of steroids and isoprenoids. In previous studies, the enzyme from pig liver was purified and characterized, and preliminary work showed that the enzyme follows hyperbolic kinetics and a sequential mechanism. The present work is a more detailed analysis of its kinetic mechanism, using initial velocity and isotope exchange at equilibrium measurements. The results are compatible with a Bi Bi sequential ordered mechanism with phosphomevalonate as the first substrate and ADP the last product. The K m values estimated are 43 ± 7 μM for Mg-ATP and 12 ± 3 μM for phosphomevalonate, with a V max of 51 ± 2 μmol min -1 mg of protein -1.

Original languageEnglish
Pages (from-to)189-196
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume454
Issue number2
DOIs
Publication statusPublished - 15 Oct 2006

Keywords

  • Isotope exchange at equilibrium
  • Kinetic mechanism
  • Phosphomevalonate kinase
  • Pig liver

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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