Evidence of essential arginyl residues in chicken liver mevalonate-5-pyrophosphate decarboxylase

Ana María Jabalquinto, Jaime Eyzaguirre, Emilio Cardemil

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

14 Citas (Scopus)

Resumen

Chicken liver mevalonate-5-pyrophosphate decarboxylase (ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33.) is inactivated by phenylglyoxal in triethanolamine buffer at pH 8.15. The reaction follows pseudo-first-order kinetics with a second-order rate constant of 108 m-1 min-1. Appropriate treatment of the kinetic data for the inactivation reaction indicates that the reaction of a single phenylglyoxal molecule per active unit of the enzyme is enough to completely inactivate the protein. The partially inactivated enzyme shows unaltered Km but decreased V as compared to native mevalonate-5-pyrophosphate decarboxylase. The dissociation constants for the enzyme-substrate complexes were estimated from inactivation reactions at different concentrations of substrates. From the data it is concluded that the modified amino acid is important for the binding of both substrates.

Idioma originalInglés
Páginas (desde-hasta)338-343
Número de páginas6
PublicaciónArchives of Biochemistry and Biophysics
Volumen225
N.º1
DOI
EstadoPublicada - ago 1983

Áreas temáticas de ASJC Scopus

  • Biofísica
  • Bioquímica
  • Biología molecular

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