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Kinetic properties and inhibition of Trypanosoma cruzi 3-hydroxy-3-methylglutaryl CoA reductase

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

  • Ramón Hurtado-Guerrrero
  • Javier Pena Diaz
  • Andrea Montalvetti
  • Luis M Ruiz-Pérez
  • Dolores González-Pacanowska

A detailed kinetic analysis of the recombinant soluble enzyme 3-hydroxy-3-methylglutaryl CoA reductase (HMGR) from Trypanosoma cruzi has been performed. The enzyme catalyzes the normal anabolic reaction and the reductant is NADPH. It also catalyzes the oxidation of mevalonate but at a lower proportion compared to the anabolic reaction. We report that the catalytically active species of HMGR in solution is the tetrameric form. Fluvastatin inhibited competitively the enzyme while cerivastatin binds by a mechanism which is more accurately described by a biphasic process characteristic of a class of 'slow, tight-binding' inhibitors.

OriginalsprogEngelsk
TidsskriftFEBS letters
Vol/bind510
Udgave nummer3
Sider (fra-til)141-4
Antal sider4
ISSN0014-5793
StatusUdgivet - 16 jan. 2002

ID: 138821727