Kinetic properties and inhibition of Trypanosoma cruzi 3-hydroxy-3-methylglutaryl CoA reductase.
FEBS Lett
; 510(3): 141-4, 2002 Jan 16.
Article
em En
| MEDLINE
| ID: mdl-11801242
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Trypanosoma cruzi
/
Inibidores de Hidroximetilglutaril-CoA Redutases
/
Hidroximetilglutaril-CoA Redutases
Idioma:
En
Ano de publicação:
2002
Tipo de documento:
Article