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MoeH 5: a natural glycorandomizer from the moenomycin biosynthetic pathway
Author(s) -
Ostash Bohdan,
Campbell Jennifer,
Luzhetskyy Andriy,
Walker Suzanne
Publication year - 2013
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12437
Subject(s) - biology , glutamine amidotransferase , biosynthesis , superfamily , gene , biochemistry , transferase , antibiotics , enzyme , streptomyces , genetics , computational biology , glutamine , microbiology and biotechnology , bacteria , amino acid
Summary The biosynthesis of the phosphoglycolipid antibiotic moenomycin A attracts the attention of researchers hoping to develop new moenomycin‐based antibiotics against multidrug resistant G ram‐positive infections. There is detailed understanding of most steps of this biosynthetic pathway in S treptomyces ghanaensis ( ATCC 14672), except for the ultimate stage, where a single pentasaccharide intermediate is converted into a set of unusually modified final products. Here we report that only one gene, moeH5 , encoding a homologue of the glutamine amidotransferase ( GAT ) enzyme superfamily, is responsible for the observed diversity of terminally decorated moenomycins. Genetic and biochemical evidence support the idea that MoeH 5 is a novel member of the GAT superfamily, whose homologues are involved in the synthesis of various secondary metabolites as well as K and O antigens of bacterial lipopolysaccharide. Our results provide insights into the mechanism of MoeH 5 and its counterparts, and give us a new tool for the diversification of phosphoglycolipid antibiotics.