 |
|
Title
|
|
Aminopeptidase from Streptomyces griseus: primary structure and comparison with other zinc-containing aminopeptidases.
|
|
|
Authors
|
|
B.Maras,
H.M.Greenblatt,
G.Shoham,
A.Spungin-Bialik,
S.Blumberg,
D.Barra.
|
|
|
Ref.
|
|
Eur J Biochem, 1996,
236,
843-846.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|