EPSILON-POLY-L-LYSINE DISPERSITY IS CONTROLLED BY A HIGHLY UNUSUAL NON-RIBOSOMAL PEPTIDE SYNTHETASE

来源 :15th International Symposiium on the Biology of Actinomycete | 被引量 : 0次 | 上传用户:jie_169
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  ε-Poly-L-lysine (ε-PL) consists of 25-35 L-lysine residues in isopeptide linkages and is one of only two amino acid homopelymers known in nature.Elucidating the biosynthetic mechanism of ε-PL should open new avenues for creating novel classes of biopolymers.We have recently reported the purification of an ε-PL synthetase (Pls:130 kDa) and the cloning of its gene from an ε -PL producing strain of Streptomyces albulus [1].Pls was found to be a membrane protein with adenylation and thiolation domains characteristic of the nonribosomal peptide synthetases (NRPSs).
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