Purification and characterization of a novel tripeptidyl aminopeptidase from Streptomyces lividans 66

FEBS Letters

Krieger, Timothy J.¹  Bartfeld, Daniel¹  Hadary, Dany¹  Jenish, David L.¹ 

[1] Cangene Corporation, 6280 Northwest Drive, Mississauga, Ontario L4V 1J7, Canada

关键词: Tripeptidyl aminopeptidase;    Recombinant protein expression;    Protein degradation;    Serine proteinase;    Fermentation Streptomyces lividans;    EPO;    recombinant human erythropoeitin;    GM-CSF;    recombinant human granulocyte macrophage colony stimulating factor;    IL-3;    recombinant human interleukin-3;    IL-6;    recombinant human N-alanyl interleukin-6;    PMSF;    phenylmethanesulfonylfluoride;    TAP;    tripeptidyl aminopeptidase;   

DOI  :  10.1016/0014-5793(94)00988-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

An extracellular tripeptidyl aminopeptidase has been purified from Streptomyces lividans 66 cell-free cultures. The enzyme is a major component of the secreted proteolytic activity. The protease removes only the N-terminal tripeptide from recombinant human GM-CSF and IL-3 but does not cleave recombinant human IL-6. The enzyme cleaves the synthetic tripeptide substrates APA-pNA and APM-pNA but does not cleave substrates with blocked amino terminals. Smaller substrates are not cleaved. The enzyme appears to be a serine protease of 55 kDa molecular weight. The pH optimum is between 7.5 and 8.5 but varies slightly with the substrate. The N-terminal sequence and amino acid composition have been determined.

【 授权许可】

Unknown