Pig liver phosphomevalonate kinase: Kinetic mechanism

Jaime Eyzaguirre, David Valdebenito, Emilio Cardemil

Resultado de la investigación: Article

10 Citas (Scopus)

Resumen

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.

Idioma originalEnglish
Páginas (desde-hasta)189-196
Número de páginas8
PublicaciónArchives of Biochemistry and Biophysics
Volumen454
N.º2
DOI
EstadoPublished - 15 oct 2006

Huella dactilar

Liver
Swine
Kinetics
Adenosine Triphosphate
Phosphorylation
Biosynthesis
Terpenes
Enzymes
Isotopes
Adenosine Diphosphate
Steroids
Substrates
phosphomevalonic acid
phosphomevalonate kinase
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Citar esto

Eyzaguirre, Jaime ; Valdebenito, David ; Cardemil, Emilio. / Pig liver phosphomevalonate kinase : Kinetic mechanism. En: Archives of Biochemistry and Biophysics. 2006 ; Vol. 454, N.º 2. pp. 189-196.
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Pig liver phosphomevalonate kinase : Kinetic mechanism. / Eyzaguirre, Jaime; Valdebenito, David; Cardemil, Emilio.

En: Archives of Biochemistry and Biophysics, Vol. 454, N.º 2, 15.10.2006, p. 189-196.

Resultado de la investigación: Article

TY - JOUR

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T2 - Kinetic mechanism

AU - Eyzaguirre, Jaime

AU - Valdebenito, David

AU - Cardemil, Emilio

PY - 2006/10/15

Y1 - 2006/10/15

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AB - 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.

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