Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase

Marysol Alvear, Ana María Jabalquinto, Jaime Eyzaguirre, Emilio Cardemil

Resultado de la investigación: Contribución a una revistaArtículo

36 Citas (Scopus)

Resumen

Mevalonate-5-pyrophosphate decarboxylase [ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33] has been purified 5800 times from chicken liver and obtained in a stable and highly purified form. The protein is a dimer of molecular weight 85 400 ± 1941, and its subunits were not resolved by gel electrophoresis in denaturing conditions. The purified enzyme does not require the presence of SH-containing reagents for either activity or stability. The enzyme shows a high specificity for adenosine 5′-triphosphate (ATP) and requires for activity a divalent metal cation, Mg2+ being most effective. The optimum pH for the enzyme ranges from 4.0 to 6.5. Inhibitory effects for the enzyme activity were detected by citrate, phthalate, and phosphate. The isoelectric point, as determined by column chromatofocusing, is 4.8. The kinetics are hyperbolic for both substrates, showing a sequential mechanism; true Km values of 0.0141 mM and 0.504 mM have been obtained for mevalonate-5-pyrophosphate and ATP, respectively.

Idioma originalInglés
Páginas (desde-hasta)4646-4650
Número de páginas5
PublicaciónBiochemistry
Volumen21
N.º19
EstadoPublicada - 1982

Áreas temáticas de ASJC Scopus

  • Bioquímica

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  • Citar esto

    Alvear, M., Jabalquinto, A. M., Eyzaguirre, J., & Cardemil, E. (1982). Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase. Biochemistry, 21(19), 4646-4650.