Phylogenetic analysis of condensation domains in NRPS sheds light on their functional evolution.

ABSTRACT:

Background

Non-ribosomal peptide synthetases (NRPSs) are large multimodular enzymes that synthesize a wide range of biologically active natural peptide compounds, of which many are pharmacologically important. Peptide bond formation is catalyzed by the Condensation (C) domain. Various functional subtypes of the C domain exist: An LCL domain catalyzes a peptide bond between two L-amino acids, a DCL domain links an L-amino acid to a growing peptide ending with a D-amino acid, a Starter C domain (first denominated and classified as a separate subtype here) acylates the first amino acid with a beta-hydroxy-carboxylic acid (typically a beta-hydroxyl fatty acid), and Heterocyclization (Cyc) domains catalyze both peptide bond formation and subsequent cyclization of cysteine, serine or thr

SUBMITTER: Rausch C 

PROVIDER: S-EPMC1894796 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature