Comparative Analysis of Signature Sequences from Adenylation Domains Situated within Bacterial-Origin Nonribosomal Peptide Synthetase Modules.

ABSTRACT: Nonribosomal peptides are assembled by large enzymes that contain multiple active sites, which function in a modular manner. The adenylation (A) domains present within typical nonribosomal peptide synthetase (NRPS) modules contain specificity-conferring codes or signature sequences (SNSs). In this study, we obtained 2051 A domain sequences from 67 bacterial species. Their alignment and clustering identified 508 SNSs. Over 80% of the SNSs displayed distinct specificity for 36 proteinogenic and nonproteinogenic α-amino acid moieties (α-AAMs). Furthermore, modifications such as N-methylation, monooxygenase activity, and oxidation contributed to the elongation of the A domains, while conferring pronounced affinities for certain α-AAMs. Notably, β-hydroxylation demonstrated particular pr

SUBMITTER: Gao W 

PROVIDER: S-EPMC12283262 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature