Molecular and Cellular Biochemistry

, Volume 280, Issue 1–2, pp 17–23 | Cite as

Pyridoxal phosphate inhibits the group I intron splicing

  • Chul Jung
  • Sook Shin
  • In Kook Park


The coenzyme pyridoxal phosphate and its analogs were tested for inhibition of the self-splicing of primary transcripts of the phage T4 thymidylate synthase gene (td). Of all compounds examined, the pyridoxal phosphate was the most potent inhibitor and the order of inhibitory efficiency for compounds tested was as follows: pyridoxal phosphate > pyridoxal > pyridoxine > pyridoxamine > pyridoxic acid. Increasing Mg2+ concentration up to 14 mM overcame the suppression of self-splicing by pyridoxal phosphate up to 95% of the level of normal splicing, implying its interference with effective catalysis of Mg2+. The kinetic analysis demonstrated that pyridoxal phosphate acts as a mixed type noncompetitive inhibitor for the td intron RNA with a Ki of 11.8 mM. The specificity of the splicing inhibition by pyridoxal phosphate is predominantly due to increases in Km and decreases in Vmax values. (Mol Cell Biochem xxx: 17–34, 2005)


group I intron noncompetitive inhibition pyridoxal phosphate self-splicing T4 phage 


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Copyright information

© Springer Science + Business Media, Inc. 2005

Authors and Affiliations

  1. 1.Department of BiologyDongguk UniversitySeoulKorea
  2. 2.Department of BiologySahmyook UniversitySeoulKorea
  3. 3.Department of BiologyDongguk UniversitySeoulKorea

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