Aminopeptidase from Streptomyces griseus
Open Access
- 1 March 1996
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 236 (3), 843-846
- https://doi.org/10.1111/j.1432-1033.1996.00843.x
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.Keywords
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