Aminopeptidase from Streptomyces griseus Primary structure and comparison with other zinc-containing aminopeptidases

Bruno Maras, Harry M. Greenblatt, Gil Shoham, Anya Spungin-Bialik, Shmaryahu Blumberg, Donatella Barra*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

52 Scopus citations

Abstract

The aminopeptidase from Streptomyces griseus is a calcium-activated metalloenzyme, which contains 2 mol tightly bound zinc/mol protein. This aminopeptidase rapidly hydrolyzes peptide bonds formed by N-terminal hydrophobic amino acids, such as leucine, methionine and phenylalanine. We have determined the complete primary structure of the protein, which contains 284 amino acid residues, yielding a molecular mass of 29723 Da. A search in the Swiss-Prot database for sequence similarities revealed a low degree of identity (26-34%) to Saccharomyces cerevisiae aminopeptidase Y, Aeromonas proteolytica aminopeptidase, and a hypothetical 49.5-kDa protein from Bacillus subtilis, which is supposed to belong to the aminopeptidase Y family. In all these proteins, the residues that are known to be involved in zinc coordination are conserved.

Original languageAmerican English
Pages (from-to)843-846
Number of pages4
JournalEuropean Journal of Biochemistry
Volume236
Issue number3
DOIs
StatePublished - 1996

Keywords

  • Metalloproteins
  • Primary structure
  • Streptomyces griseus
  • Zinc-containing aminopeptidases

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