Analysis of 51 cyclodipeptide synthases reveals the basis for substrate specificity.
Nat Chem Biol
; 11(9): 721-7, 2015 Sep.
Article
em En
| MEDLINE
| ID: mdl-26236937
ABSTRACT
Cyclodipeptide synthases (CDPSs) constitute a family of peptide bond-forming enzymes that use aminoacyl-tRNAs for the synthesis of cyclodipeptides. Here, we describe the activity of 41 new CDPSs. We also show that CDPSs can be classified into two main phylogenetically distinct subfamilies characterized by specific functional subsequence signatures, named NYH and XYP. All 11 previously characterized CDPSs belong to the NYH subfamily, suggesting that further special features may be yet to be discovered in the other subfamily. CDPSs synthesize a large diversity of cyclodipeptides made up of 17 proteinogenic amino acids. The identification of several CDPSs having the same specificity led us to determine specificity sequence motifs that, in combination with the phylogenetic distribution of CDPSs, provide a first step toward being able to predict the cyclodipeptides synthesized by newly discovered CDPSs. The determination of the activity of ten more CDPSs with predicted functions constitutes a first experimental validation of this predictive approach.
Texto completo:
1
Coleções:
01-internacional
Contexto em Saúde:
3_ND
Base de dados:
MEDLINE
Assunto principal:
Peptídeo Sintases
/
Peptídeos Cíclicos
/
Proteínas de Bactérias
/
Proteínas Fúngicas
/
Dipeptídeos
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Nat Chem Biol
Ano de publicação:
2015
Tipo de documento:
Article