e-Poly-L-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase

@inproceedings{Yamanaka2008ePolyLlysineDI,
  title={e-Poly-L-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase},
  author={Kazuya Yamanaka and Chitose Maruyama and Hiroshi Takagi and Yoshimitsu Hamano},
  year={2008}
}
e-Poly-L-lysine (e-PL) consists of 25–35 L-lysine residues in isopeptide linkages and is one of only two amino acid homopolymers known in nature. Elucidating the biosynthetic mechanism of e-PL should open new avenues for creating novel classes of biopolymers. Here we report the purification of an e-PL synthetase (Pls; 130 kDa) and the cloning of its gene from an e-PL–producing strain of Streptomyces albulus. Pls was found to be a membrane protein with adenylation and thiolation domains… CONTINUE READING