Vioserpin, a serine protease inhibitor from Gloeobacter violaceus possibly regulated by heparin

Biochimie. 2016 Aug:127:115-20. doi: 10.1016/j.biochi.2016.05.006. Epub 2016 May 6.

Abstract

Serine peptidase inhibitor (serpin) is the name given to the superfamily of proteins with wide range of biological functions, and that the main feature is the inhibition of serine proteases. Here we describe the inhibitory characterization of a serpin from Gloeobacter violaceus that we named vioserpin. The serpin presented a high specificity to inhibit trypsin-like enzymes with a rapid inhibition rate constant (2.1 × 10(6) M(-1) s(-1)). We also demonstrated that the inhibitory activity of the vioserpin is influenced by the concentration of heparin, and this finding may throw a new light on understanding the molecular evolution of serpins.

Keywords: Bacterial serpin; Gloeobacter violaceus; Protease inhibitor; Serine peptidase; Serpin; Vioserpin.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Cyanobacteria*
  • Heparin / metabolism*
  • Humans
  • Kinetics
  • Mice
  • Phylogeny
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Recombinant Proteins / pharmacology
  • Serine Proteinase Inhibitors / chemistry
  • Serine Proteinase Inhibitors / isolation & purification
  • Serine Proteinase Inhibitors / metabolism
  • Serine Proteinase Inhibitors / pharmacology*
  • Trypsin / metabolism

Substances

  • Recombinant Proteins
  • Serine Proteinase Inhibitors
  • Heparin
  • Trypsin