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

Alejandro Venegas, Joseph Martial, Pablo Valenzuela

Research output: Contribution to journalArticlepeer-review

41 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1053-1059
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume55
Issue number4
DOIs
Publication statusPublished - 19 Dec 1973

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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