Abstract

Polyketide synthase (PKSs) and nonribosomal peptide synthetase (NRPSs) arelarge multimodular enzymes involved in biosynthesis of polyketide and peptide toxinsproduced by fungi. Furthermore, hybrid enzymes, in which a reducing PKS region is fusedto a single NRPS module, are also responsible of the synthesis of peptide-polyketidemetabolites in fungi. The genes encoding for PKSs and NRPSs have been exposed tocomplex evolutionary mechanisms, which have determined the great number and diversityof metabolites. In this study, we considered the most important polyketide and peptidemycotoxins and, for the first time, a phylogenetic analysis of both PKSs and NRPSsinvolved in their biosynthesis was assessed using two domains for each enzyme:?-ketosynthase (KS) and acyl-transferase (AT) for PKSs; adenylation (A) andcondensation (C) for NRPSs. The analysis of both KS and AT domains confirmed thedifferentiation of the three classes of highly, partially and non-reducing PKSs. HybridPKS-NRPSs involved in mycotoxins biosynthesis grouped together in the phylogenetictrees of all the domains analyzed. For most mycotoxins, the corresponding biosyntheticenzymes from distinct fungal species grouped together, except for PKS and NRPSinvolved in ochratoxin A biosynthesis, for which an unlike process of evolution could behypothesized in different species.

Autore Pugliese

• Perrone Giancarlo , Ferrara Massimo , Gallo Antonia

Tutti gli autori

• Gallo A.; Ferrara M.; Perrone G.

Titolo volume/Rivista

Toxins

Anno di pubblicazione

2013

ISSN

2072-6651

ISBN

Non Disponibile

Numero di citazioni Wos

Nessuna citazione

Ultimo Aggiornamento Citazioni

Non Disponibile

Numero di citazioni Scopus

Non Disponibile

Ultimo Aggiornamento Citazioni

Non Disponibile

Settori ERC

Non Disponibile

Codici ASJC

Non Disponibile