Occurrence of epsilon-poly-L-lysine-degrading enzyme in epsilon-poly-L-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization.
Epsilon-poly-L-lysine (epsilon-PL)-degrading enzyme was found in the epsilon-PL-tolerant strain Sphingobacterium multivorum OJ10 and purified to homogeneity. The purified enzyme has a molecular mass of approximately 80 kDa. The enzyme catalyzed exo-type degradation of epsilon-PL and released L-lysine. The enzyme was a Co2+ or Ca2+ ion-activated aminopeptidase.
Kito
Mitsuaki
M
Department of Biomolecular Science, Faculty of Engineering, Gifu University, Yanagido, 501-1193, Gifu, Japan.
Onji
Yuichi
Y
Yoshida
Toyokazu
T
Nagasawa
Toru
T
D000626:Aminopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D005417:Flavobacterium / Q000201:enzymology* / Q000302:isolation & purification; D008970:Molecular Weight; D011107:Polylysine / Q000378:metabolism*; D013379:Substrate Specificity
D011107:Polylysine; D000626:Aminopeptidases