Macrolactonization catalyzed by the terminal thioesterase domain of the nonribosomal peptide synthetase responsible for lichenysin biosynthesis.
The excised terminal thioesterase of the lichenysin nonribosomal peptide synthetase was found to be a highly efficient and versatile enzyme. Its activity strictly requires the R configuration of the beta-hydroxy fatty acid and the side chains of aspartate-5 and isoleucine-7, but tolerates changes in five other residues of the substrate. Characterization of this enzyme facilitates future effort to engineer the lichenysin synthetase for biotechnological applications.
Cao
Shuyong
S
Department of Chemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.
Yang
Yanzhen
Y
Ng
Na Lee Joyce
NL
Guo
Zhihong
Z
D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D004950:Esterases / Q000737:chemistry*; D007700:Kinetics; D007783:Lactones / Q000737:chemistry*; D008074:Lipoproteins / Q000138:chemical synthesis*; D010453:Peptide Synthases / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000138:chemical synthesis*
D007783:Lactones; D008074:Lipoproteins; D010456:Peptides, Cyclic; C094325:lichenysin A; D004950:Esterases; D010453:Peptide Synthases