TAILIEUCHUNG - Báo cáo khoa học: In silico analysis of the adenylation domains of the freestanding enzymes belonging to the eucaryotic nonribosomal peptide synthetase-like family

This work presents a computational analysis of the molecular characteris-tics shared by the adenylation domains from traditional nonribosomal pep-tide synthetases (NRPSs) and the group of the freestanding homologous enzymes: a-aminoadipate semialdehyde dehydrogenase, a-aminoadipate reductase and the protein Ebony. The results of systematic sequence com-parisons allow us to conclude that a specificity-conferring code, similar to that described for the NRPSs, can be recognized in such enzymes. | ềFEBS Journal In silico analysis of the adenylation domains of the freestanding enzymes belonging to the eucaryotic nonribosomal peptide synthetase-like family Leonardo Di Vincenzo1 Ingeborg Grgurina1 and Stefano Pascarella1 2 1 Dipartimento di Scienze Biochimiche A. Rossi Fanelli Universita di Roma La Sapienza Roma Italy 2 Centro Interdipartimentale di Ricerca per l Analisi dei Modelli e dell Informazione nei Sistemi Biomedici CISB Universita di Roma La Sapienza Roma Italy Keywords nonribosomalpeptide synthetase homology modelling docking specifity conferring code freestanding NRPSs Correspondence S. Pascarella Dipartimento di Scienze Biochimiche A. Rossi Fanelli University di Roma La Sapienza 00185 Roma Italy Fax 39 06 49917566 Tel 39 06 49917574 E-mail Website http bio_chem Received 8 August 2004 revised 30 November 2004 accepted 9 December 2004 This work presents a computational analysis of the molecular characteristics shared by the adenylation domains from traditional nonribosomal peptide synthetases NRPSs and the group of the freestanding homologous enzymes a-aminoadipate semialdehyde dehydrogenase a-aminoadipate reductase and the protein Ebony. The results of systematic sequence comparisons allow us to conclude that a specificity-conferring code similar to that described for the NRPSs can be recognized in such enzymes. The structural and functional roles of the residues involved in the substrate selection and binding are proposed through the analysis of the predicted interactions of the model active sites and their respective substrates. The indications deriving from this study can be useful for the programming of experiments aimed at a better characterization and at the engineering of this emerging group of single NRPS modules that are responsible for amino acid selection activation and modification in the absence of other NRPS assembly line components. doi .

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