Aminopeptidase from Streptomyces griseus: primary structure and comparison with other zinc-containing aminopeptidases.
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Maras B, Greenblatt HM, Shoham G, Spungin-Bialik A, Blumberg S, Barra D
Aminopeptidase from Streptomyces griseus: primary structure and comparison with other zinc-containing aminopeptidases.
Eur J Biochem. 1996 Mar 15;236(3):843-6.
- PubMed ID
- 8665903 [ View in PubMed]
- 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.