A novel subclassification for Kunitz proteinase inhibitors from leguminous seeds

Biochimie. 2010 Nov;92(11):1667-73. doi: 10.1016/j.biochi.2010.03.021. Epub 2010 Apr 2.

Abstract

Kunitz-type trypsin inhibitors from legume seeds have been characterized structurally. The presence of Cys-Cys in single or double chains shows a new pattern of proteins structurally not so closely related to STI. Therefore, briefly, with regard to cysteine content, plant Kunitz proteinase inhibitors may be classified into four groups: no Cys-Cys at all, one, two and more than two Cys residues. Functional properties and diversity of these proteins are also briefly discussed.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Cysteine
  • Fabaceae*
  • Humans
  • Molecular Sequence Data
  • Peptide Hydrolases / metabolism*
  • Peptides / chemistry
  • Peptides / classification*
  • Peptides / metabolism
  • Plant Proteins / chemistry
  • Plant Proteins / classification*
  • Plant Proteins / metabolism
  • Protein Conformation
  • Seeds*

Substances

  • Kunitz-type protease inhibitor, plant
  • Peptides
  • Plant Proteins
  • Peptide Hydrolases
  • Cysteine