A derivative of the glycopeptide A40926 produced by inactivation of the β-hydroxylase gene in Nonomuraea sp. ATCC39727.

Autor: Stinchi, Sofia, Carrano, Lucia, Lazzarini, Ameriga, Feroggio, Marina, Grigoletto, Armando, Sosio, Margherita, Donadio, Stefano
Předmět:
Zdroj: FEMS Microbiology Letters; Mar2006, Vol. 256 Issue 2, p229-235, 7p, 2 Diagrams
Abstrakt: The actinomycete Nonomuraea sp. ATCC39727 produces the glycopeptide A40926. In the corresponding dbv cluster, ORF28 encodes a putative hydroxylase. A gene replacement mutant of ORF28 in Nonomuraea produces a small amount of an A40926-related metabolite, 16 amu smaller than the parent compound, which was identified as the desoxyderivative of A40926 lacking the β-hydroxyl group on the tyrosine moiety. This result demonstrates that ORF28 is actually involved in the formation of the β-hydroxytyrosine residue present in A40926. The formation of an altered glycopeptide and the inability to rescue A40926 production upon feeding free β-hydroxytyrosine are consistent with the possibility that, in contrast to balhimycin formation, hydroxylation occurs after tyrosine activation by the nonribosomal peptide synthetase. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index