Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
21611 | Journal of Bioscience and Bioengineering | 2011 | 4 Pages |
Abstract
ABSTRACTε-Poly-L-lysine (ε-PL) synthetase (Pls), which is a membrane protein with adenylation and thiolation domains characteristic of the nonribosomal peptide synthetases, catalyzes polymerization of L-lysine molecules (25-mer to 35-mer). Here, we report on the development of a recombinant Pls expression system that allowed us to perform a site-directed mutational analysis.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Kazuya Yamanaka, Naoko Kito, Akihiro Kita, Yuuki Imokawa, Chitose Maruyama, Takashi Utagawa, Yoshimitsu Hamano,