The modified amino acids 2,4-diaminobutyric acid, (2,4 Dab) 2,3-dehydroaminobutyric acid (2,3 Dhb) are present in lipopeptides syringopeptins and lipodespinonapeptides (LDNPs) produced by the phytopathogenic bacterium Pseudomonas syringae pv. syringae. LDNPs contain also 3-hydroxy-aspartic acid (3-OH)Asp and 4-chlorothreonine (4-Cl) Thr. Feeding 14CThr and 14CAsp to chloramphenicol containing bacterial cultures produced radioactively labelled lipopeptide metabolites. Degradation studies showed that Thr is the biosynthetic precursor of (4-Cl)Thr and 2,3-Dhb, while Asp, besides labelling the above residues, is also incorporated in (3-OH)Asp and 2,4-Dab.
Biosynthetic origin of four modified aminoacidic residues in bioactive lipodepsipeptides prom Pseudomonas syringae pv. syringae / Grgurina, Ingeborg; F., Mariotti. - STAMPA. - (1995), pp. 125-125. (Intervento presentato al convegno 40° Congresso Nazionale della Società Italiana di Biochimica tenutosi a TORINO nel 12-15 Sept).
Biosynthetic origin of four modified aminoacidic residues in bioactive lipodepsipeptides prom Pseudomonas syringae pv. syringae
GRGURINA, Ingeborg;
1995
Abstract
The modified amino acids 2,4-diaminobutyric acid, (2,4 Dab) 2,3-dehydroaminobutyric acid (2,3 Dhb) are present in lipopeptides syringopeptins and lipodespinonapeptides (LDNPs) produced by the phytopathogenic bacterium Pseudomonas syringae pv. syringae. LDNPs contain also 3-hydroxy-aspartic acid (3-OH)Asp and 4-chlorothreonine (4-Cl) Thr. Feeding 14CThr and 14CAsp to chloramphenicol containing bacterial cultures produced radioactively labelled lipopeptide metabolites. Degradation studies showed that Thr is the biosynthetic precursor of (4-Cl)Thr and 2,3-Dhb, while Asp, besides labelling the above residues, is also incorporated in (3-OH)Asp and 2,4-Dab.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
