Inhibition of rat brain galactocerebroside sulfotransferase by triazine aromatic dyes: interaction with the 3'-phosphoadenosine 5'-phosphosulfate binding site

Biochem Biophys Res Commun. 1985 Jun 14;129(2):522-9. doi: 10.1016/0006-291x(85)90183-4.

Abstract

The mechanism of inhibition of rat brain cerebroside sulfotransferase (EC 2.8.2.11) by a series of triazine aromatic dyes was examined. These dyes are putative site-specific probes of the "dinucleotide fold". All of the dyes examined were competitive inhibitors of cerebroside sulfotransferase with respect to 3'-phosphoadenosine 5'-phosphosulfate (PAPS) binding. In addition, the binding of the dye, Congo Red, to the sulfotransferase was associated with a red shift in its absorption spectrum. Based on these results, it is suggested that rat brain cerebroside sulfotransferase contains a "dinucleotide fold" as a structural feature of the protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenine Nucleotides / metabolism*
  • Animals
  • Binding Sites
  • Brain / enzymology*
  • Coloring Agents / pharmacology
  • In Vitro Techniques
  • Phosphoadenosine Phosphosulfate / metabolism*
  • Protein Conformation
  • Rats
  • Sulfotransferases*
  • Sulfurtransferases / antagonists & inhibitors*
  • Sulfurtransferases / metabolism
  • Triazines / pharmacology*

Substances

  • Adenine Nucleotides
  • Coloring Agents
  • Triazines
  • Phosphoadenosine Phosphosulfate
  • Cibacron Blue F 3GA
  • Sulfurtransferases
  • Sulfotransferases
  • galactosylceramide sulfotransferase