The 92-kDa chitinase from Streptomyces olivaceoviridis contains a lysine-C endoproteinase at its N-terminus.
Serine proteinases of 42, 22 and 14 kDa were purified from the culture fluid of Streptomyces olivaceoviridis by FPLC. The first 14 amino acids at their N-termini were identical and coincide with the N-terminal amino acid sequence of 92-kDa chitinase, which was found to hydrolyse casein. The four proteins hydrolyse synthetic substrates at the carboxyl group of lysine and (more slowly) arginine. The 14-kDa endoproteinase releases only two fragments of 42 and 43 kDa from beta-galactosidase. When the pure 92-kDa chitinase was incubated at 37 degrees C in Tris.HCl buffer, it was cleaved into a 70-kDa chitinase and a 22-kDa proteinase which in its part is rapidly degraded to a 14-kDa proteinase.
Radwan
H H
HH
Institut für Mikrobiologie, Universität Hannover, FRG.
Plattner
H J
HJ
Menge
U
U
Diekmann
H
H
D000595:Amino Acid Sequence; D002688:Chitinases / Q000737:chemistry*; D010450:Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D008969:Molecular Sequence Data; D013302:Streptomyces / Q000201:enzymology*
D002688:Chitinases; D010450:Endopeptidases; C044574:lysine-C peptidase