title: Mutational analysis of the three tandem domains of ε-poly-L-lysine synthetase catalyzing the L-lysine polymerization reaction.
abstract: ε-Poly-l-lysine (ε-PL) synthetase (Pls) is a nonribosomal peptide synthetase (NRPS)-like enzyme with three tandem domains to catalyze the l-lysine polymerization reaction. Mutational analysis of the three tandem domains demonstrated that the interconnected action of all three domains is essential for the enzyme activity.
authors.affiliation: Department of Bioscience, Fukui Prefectural University, 4-1-1 Matsuoka-Kenjojima, Eiheiji-cho, Yoshida-gun, Fukui 910-1195, Japan.
authors.forename: Naoko
authors.initials: N
authors.lastname: Kito
authors.forename: Chitose
authors.initials: C
authors.lastname: Maruyama
authors.forename: Kazuya
authors.initials: K
authors.lastname: Yamanaka
authors.forename: Yuuki
authors.initials: Y
authors.lastname: Imokawa
authors.forename: Takashi
authors.initials: T
authors.lastname: Utagawa
authors.forename: Yoshimitsu
authors.initials: Y
authors.lastname: Hamano
mesh_terms: D000595:Amino Acid Sequence; D055162:Biocatalysis; D008239:Lysine / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D010453:Peptide Synthases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011107:Polylysine / Q000096:biosynthesis* / Q000737:chemistry; D058105:Polymerization; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D013302:Streptomyces / Q000201:enzymology
chemical_list: D011107:Polylysine; D010453:Peptide Synthases; C104385:non-ribosomal peptide synthase; D008239:Lysine