Cystatins, serpins and other families of protease inhibitors in plants

Curr Protein Pept Sci. 2011 Aug;12(5):386-98. doi: 10.2174/138920311796391098.

Abstract

Plant protease inhibitors (PIs) are generally small proteins present in high concentrations in storage tissues (tubers and seeds), and to a lower level in leaves. Even if most of them are active against serine and cysteine proteases, PIs active against aspartic proteases and carboxypeptidases have also been identified. Inhibitors of serine proteases are further classifiable in several families on the basis of their structural features. They comprise the families known as Bowman-Birk, Kunitz, Potato I and Potato II, which are the subject of review articles included in this special issue. In the present article we aim to give an overview of other families of plant PIs, active either against serine proteases or other class of proteases, describing their distribution, activity and main structural characteristics.

Publication types

  • Review

MeSH terms

  • Aspartic Acid Proteases / antagonists & inhibitors
  • Cystatins / chemistry
  • Cystatins / metabolism*
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism*
  • Protease Inhibitors / chemistry
  • Protease Inhibitors / metabolism*
  • Serpins / chemistry
  • Serpins / metabolism*
  • Trypsin Inhibitors / chemistry
  • Trypsin Inhibitors / metabolism
  • alpha-Amylases / antagonists & inhibitors

Substances

  • Cystatins
  • Plant Proteins
  • Protease Inhibitors
  • Serpins
  • Trypsin Inhibitors
  • alpha-Amylases
  • Aspartic Acid Proteases