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Occurrence of epsilon-poly-L-lysine-degrading enzyme in epsilon-poly-L-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization. 2002

Mitsuaki Kito, and Yuichi Onji, and Toyokazu Yoshida, and Toru Nagasawa
Department of Biomolecular Science, Faculty of Engineering, Gifu University, Yanagido, 501-1193, Gifu, Japan.

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.

UI MeSH Term Description Entries
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D011107 Polylysine A peptide which is a homopolymer of lysine. Epsilon-Polylysine,Poly-(Alpha-L-Lysine),Epsilon Polylysine
D005417 Flavobacterium A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in SOIL and WATER. Its organisms are also found in raw meats, MILK and other FOOD, hospital environments, and human clinical specimens. Some species are pathogenic in humans.
D000626 Aminopeptidases A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11. Aminopeptidase
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities

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