Macrolactonization catalyzed by the terminal thioesterase domain of the nonribosomal peptide synthetase responsible for lichenysin biosynthesis.

Shuyong Cao, Yanzhen Yang, Na Lee Joyce Ng, Zhihong Guo
Author Information
  1. Shuyong Cao: Department of Chemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.

Abstract

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.

MeSH Term

Catalysis
Chromatography, High Pressure Liquid
Esterases
Kinetics
Lactones
Lipoproteins
Peptide Synthases
Peptides, Cyclic

Chemicals

Lactones
Lipoproteins
Peptides, Cyclic
lichenysin A
Esterases
Peptide Synthases

Word Cloud

Created with Highcharts 10.0.0lichenysinsynthetaseterminalthioesterasenonribosomalpeptideenzymeexcisedfoundhighlyefficientversatileactivitystrictlyrequiresRconfigurationbeta-hydroxyfattyacidsidechainsaspartate-5isoleucine-7tolerateschangesfiveresiduessubstrateCharacterizationfacilitatesfutureeffortengineerbiotechnologicalapplicationsMacrolactonizationcatalyzeddomainresponsiblebiosynthesis

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