Homology modelling of the adenylation domains present in the nonribosomal peptide synthetases involved in the biosynthesis of syringomycin and substrate docking experiments allowed to identify the residues lining the enzyme active sites that are relevant for the interaction with substrate amino acids. The specific molecular recognition fo the L-isomer of the substrate amino acids accounts for the observed stereospecificity of these domains.
"In silico" studies of the substrate specificity of the adenylation domains of syringomycin synthetase / P., Giovannini; Pascarella, Stefano; Grgurina, Ingeborg. - (2002), pp. 390-390. (Intervento presentato al convegno 23rd international Symposium on the Chemistry of Natural Products tenutosi a FLORENCE, ITALY nel 28 July- 3 August).
"In silico" studies of the substrate specificity of the adenylation domains of syringomycin synthetase
PASCARELLA, Stefano;GRGURINA, Ingeborg
2002
Abstract
Homology modelling of the adenylation domains present in the nonribosomal peptide synthetases involved in the biosynthesis of syringomycin and substrate docking experiments allowed to identify the residues lining the enzyme active sites that are relevant for the interaction with substrate amino acids. The specific molecular recognition fo the L-isomer of the substrate amino acids accounts for the observed stereospecificity of these domains.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
