Open AccessA derivative of the glycopeptide A40926 produced by inactivation of the β‐hydroxylase gene in Nonomuraea sp . ATCC39727
Author(s) -
Stinchi Sofia,
Carrano Lucia,
Lazzarini Ameriga,
Feroggio Marina,
Grigoletto Armando,
Sosio Margherita,
Donadio Stefano
Publication year - 2006
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2006.00120.x
Subject(s) - glycopeptide , gene , derivative (finance) , biochemistry , chemistry , genetics , biology , antibiotics , financial economics , economics
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.