Amino acid sequence of the protease inhibitor BWI-4a from buckwheat seeds

IUBMB Life. 2000 Apr;49(4):273-6. doi: 10.1080/15216540050033122.

Abstract

The complete amino acid sequence of protease inhibitor BWI-4a from buckwheat (Fagopyrum esculentum Moench) seeds, consisting of 67 amino acid residues with a single disulfide bond, has been established by Edman degradation in combination with matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Its N terminus is blocked by a pyroglutamic acid residue. Mass spectrometric analysis revealed that inhibitor BWI-4a is present in buckwheat seeds in two isoforms with a single amino acid substitution of Ala40 for Gly40. The reactive site of the inhibitor contains an Arg43-Asp44 bond. Analysis of the amino acid sequence suggests that the buckwheat seed protease inhibitor is a member of the potato proteinase inhibitor I family.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alanine / chemistry
  • Amino Acid Sequence
  • Binding Sites
  • Chymotrypsin / metabolism
  • Disulfides
  • Fagopyrum / chemistry*
  • Glycine / chemistry
  • Leucine / chemistry
  • Mass Spectrometry
  • Molecular Sequence Data
  • Peptides / chemistry
  • Plant Proteins / chemistry*
  • Protein Isoforms
  • Pyrrolidonecarboxylic Acid / chemistry
  • Sequence Homology, Amino Acid
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Trypsin / metabolism
  • Trypsin Inhibitors / chemistry
  • Trypsin Inhibitors / pharmacology

Substances

  • Disulfides
  • Peptides
  • Plant Proteins
  • Protein Isoforms
  • Trypsin Inhibitors
  • buckwheat inhibitor 4a
  • proteinase inhibitor I (plants)
  • Chymotrypsin
  • Trypsin
  • Leucine
  • Alanine
  • Pyrrolidonecarboxylic Acid
  • Glycine