Amino acid sequence and disulfide bridges of an antifungal protein isolated from Aspergillus giganteus

Eur J Biochem. 1990 Oct 5;193(1):31-8. doi: 10.1111/j.1432-1033.1990.tb19300.x.

Abstract

A very basic secreted protein which displays antifungal activity was isolated from the medium of the mold Aspergillus giganteus. The protein consists of 51 amino acid residues whose sequence was determined as Ala-Thr-Tyr-Asn-Gly-Lys-Cys-Tyr-Lys-Lys-Asp-Asn- Ile-Cys-Lys-Tyr-Lys-Ala-Gln-Ser-Gly-Lys-Thr-Ala-Ile-Cys-Lys-Cys-Tyr-Val- Lys- Lys-Cys-Pro-Arg-Asp-Gly-Ala-Lys-Cys-Glu-Phe-Asp-Ser-Tyr-Lys-Gly-Lys-Cys- Tyr-Cys . Disulfide bonds were formed between Cys7-Cys33, Cys14-Cys40, Cys26-Cys28 and Cys49-Cys51. These results suggest that the antifungal protein forms a loop structure and is similar to phospholipase A2.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Antifungal Agents / isolation & purification*
  • Aspergillus*
  • Chromatography, High Pressure Liquid
  • Disulfides / analysis
  • Fungal Proteins / chemistry
  • Fungal Proteins / isolation & purification*
  • Molecular Sequence Data
  • Peptide Mapping
  • Phospholipases A / chemistry
  • Phospholipases A2

Substances

  • Antifungal Agents
  • Disulfides
  • Fungal Proteins
  • antifungal protein, Aspergillus
  • Phospholipases A
  • Phospholipases A2