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Literature DB >> 21388875

Development of a recombinant ε-poly-L-lysine synthetase expression system to perform mutational analysis.

Kazuya Yamanaka¹, Naoko Kito, Akihiro Kita, Yuuki Imokawa, Chitose Maruyama, Takashi Utagawa, Yoshimitsu Hamano.

Abstract

ε-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.

Entities: Chemical

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Year: 2011 PMID： 21388875 DOI： 10.1016/j.jbiosc.2011.01.020

Source DB: PubMed Journal: J Biosci Bioeng ISSN： 1347-4421 Impact factor: 2.894

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Cited

4 in total

1. ε-Poly-L-lysine peptide chain length regulated by the linkers connecting the transmembrane domains of ε-Poly-L-lysine synthetase.

Authors: Yoshimitsu Hamano; Naoko Kito; Akihiro Kita; Yuuki Imokawa; Kazuya Yamanaka; Chitose Maruyama; Hajime Katano
Journal: Appl Environ Microbiol Date: 2014-06-06 Impact factor: 4.792

Development of a recombinant ε-poly-L-lysine synthetase expression system to perform mutational analysis.

1. ε-Poly-L-lysine peptide chain length regulated by the linkers connecting the transmembrane domains of ε-Poly-L-lysine synthetase.

2. Heterologous Production of Hyaluronic Acid in an ε-Poly-L-Lysine Producer, Streptomyces albulus.

Review 3. Recent advances in microbial ε-poly-L-lysine fermentation and its diverse applications.

4. Systematic unravelling of the biosynthesis of poly (L-diaminopropionic acid) in Streptomyces albulus PD-1.