| Literature DB >> 11958932 |
Mitsuaki Kito1, Yuichi Onji, Toyokazu Yoshida, Toru Nagasawa.
Abstract
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.Entities:
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Year: 2002 PMID: 11958932 DOI: 10.1111/j.1574-6968.2002.tb11043.x
Source DB: PubMed Journal: FEMS Microbiol Lett ISSN: 0378-1097 Impact factor: 2.742