Proteolytic enzymes from recombinant Streptomyces lividans TK24.
Different proteases from the culture fluids of recombinant Streptomyces lividans strains were isolated. Several individual proteases were separated and characterized. A chymotrypsin-chylike activity (CLA) was identified that specifically degrades a fusion protein between the alpha-amylase inhibitor from S. tendae (Tendamistat, HOE467) and proinsulin from the monkey Macaca fascicularis. The effective chemical inhibition of the degrading enzyme is demonstrated.
Aretz
W
W
Hoechst AG, Frankfurt/Main, F.R.G.
Koller
K P
KP
Riess
G
G
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism; D002852:Chromatography, Ion Exchange; D002918:Chymotrypsin / Q000037:antagonists & inhibitors / Q000378:metabolism; D008670:Metals / Q000494:pharmacology; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D013997:Time Factors
D001426:Bacterial Proteins; D008670:Metals; D011993:Recombinant Fusion Proteins; D010447:Peptide Hydrolases; D002918:Chymotrypsin