Beschreibung:
<jats:title>ABSTRACT</jats:title>
<jats:p>
Microcin C (McC), an inhibitor of the growth of enteric bacteria, consists of a heptapeptide with a modified AMP residue attached to the backbone of the C-terminal aspartate through an
<jats:italic>N</jats:italic>
-acyl phosphamidate bond. Here we identify maturation intermediates produced by cells lacking individual
<jats:italic>mcc</jats:italic>
McC biosynthesis genes. We show that the products of the
<jats:italic>mccD</jats:italic>
and
<jats:italic>mccE</jats:italic>
genes are required for attachment of a 3-aminopropyl group to the phosphate of McC and that this group increases the potency of inhibition of the McC target, aspartyl-tRNA synthetase.
</jats:p>