Active site-directed inhibition of E. coli DNA-dependent RNA polymerase by pyridoxal 5′-phosphate

Alejandro Venegas, Joseph Martial, Pablo Valenzuela

Resultado de la investigación: Article

39 Citas (Scopus)

Resumen

DNA-dependent RNA polymerase from E. coli is rapidly inhibited by preincubation with pyridoxal 5′-phosphate. The enzyme is not inhibited by pyridoxamine 5′-phosphate or pyridoxine. Pyridoxal is about 10 times less effective than pyridoxal 5′-phosphate. Nucleoside triphosphates but not DNA, protect the enzyme from inhibition. Spectral data from the reaction mixture and NaBH4 reduction products indicate the formation of a Schiff base between the aldehyde group of pyridoxal 5′-phosphate and amino group of the enzyme. The results show that the inhibitor is reacting with a critical amino group presumably at the nucleoside phosphate binding site of the active center of the enzyme.

Idioma originalEnglish
Páginas (desde-hasta)1053-1059
Número de páginas7
PublicaciónBiochemical and Biophysical Research Communications
Volumen55
N.º4
DOI
EstadoPublished - 19 dic 1973

Huella dactilar

Pyridoxal Phosphate
DNA-Directed RNA Polymerases
Escherichia coli
Catalytic Domain
Enzymes
Nucleosides
Phosphates
Pyridoxamine
Pyridoxal
Pyridoxine
Schiff Bases
Aldehydes
Binding Sites
DNA

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Medicine(all)
  • Molecular Biology
  • Cell Biology

Citar esto

Venegas, Alejandro ; Martial, Joseph ; Valenzuela, Pablo. / Active site-directed inhibition of E. coli DNA-dependent RNA polymerase by pyridoxal 5′-phosphate. En: Biochemical and Biophysical Research Communications. 1973 ; Vol. 55, N.º 4. pp. 1053-1059.
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Active site-directed inhibition of E. coli DNA-dependent RNA polymerase by pyridoxal 5′-phosphate. / Venegas, Alejandro; Martial, Joseph; Valenzuela, Pablo.

En: Biochemical and Biophysical Research Communications, Vol. 55, N.º 4, 19.12.1973, p. 1053-1059.

Resultado de la investigación: Article

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AU - Martial, Joseph

AU - Valenzuela, Pablo

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AB - DNA-dependent RNA polymerase from E. coli is rapidly inhibited by preincubation with pyridoxal 5′-phosphate. The enzyme is not inhibited by pyridoxamine 5′-phosphate or pyridoxine. Pyridoxal is about 10 times less effective than pyridoxal 5′-phosphate. Nucleoside triphosphates but not DNA, protect the enzyme from inhibition. Spectral data from the reaction mixture and NaBH4 reduction products indicate the formation of a Schiff base between the aldehyde group of pyridoxal 5′-phosphate and amino group of the enzyme. The results show that the inhibitor is reacting with a critical amino group presumably at the nucleoside phosphate binding site of the active center of the enzyme.

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