Aminopeptidase from Streptomyces griseus: primary structure and comparison with other zinc-containing aminopeptidases.
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.
Maras
B
B
Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Università La Sapienza, Roma, Italy.
Greenblatt
H M
HM
Shoham
G
G
Spungin-Bialik
A
A
Blumberg
S
S
Barra
D
D
D000333:Aeromonas / Q000201:enzymology; D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D001412:Bacillus subtilis / Q000201:enzymology; D007256:Information Systems; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D017386:Sequence Homology, Amino Acid; D013305:Streptomyces griseus / Q000201:enzymology*; D013379:Substrate Specificity; D009626:Terminology as Topic; D015032:Zinc / Q000032:analysis* / Q000378:metabolism
D000626:Aminopeptidases; C056860:lysyl aminopeptidase; D015032:Zinc