Intracellular aminopeptidases in Streptomyces lividans 66.
We have investigated the aminopeptidase activities present in Streptomyces lividans strains. The majority of these activities proved to be intracellular with multiple active species. Two aminopeptidase P genes were identified to be responsible for the ability to hydrolyze amino terminal peptide bonds adjacent to proline residues. Two other broad spectrum aminopeptidases were found to display homology at both the DNA and protein levels. One showed significant homology to PepN proteins, particularly around the putative zinc-binding residues which are important for catalysis. The second broad spectrum activity was not analyzed in detail but showed a different spectrum of substrate specificity to that of PepN.
Butler
M J
MJ
Cangene Corporation, Mississauga, Ontario, Canada.
Aphale
J S
JS
DiZonno
M A
MA
Krygsman
P
P
Walczyk
E
E
Malek
L T
LT
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D001709:Biotechnology; D018826:CD13 Antigens; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000235:genetics; D004151:Dipeptides / Q000737:chemistry; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D015183:Restriction Mapping; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid; D013302:Streptomyces / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity
D004269:DNA, Bacterial; D004151:Dipeptides; D000626:Aminopeptidases; D018826:CD13 Antigens; C022750:X-Pro aminopeptidase