Ontology highlight
ABSTRACT:
SUBMITTER: Koehnke J
PROVIDER: S-EPMC4512242 | biostudies-literature | 2015 Aug
REPOSITORIES: biostudies-literature
Koehnke Jesko J Mann Greg G Bent Andrew F AF Ludewig Hannes H Shirran Sally S Botting Catherine C Lebl Tomas T Houssen Wael W Jaspars Marcel M Naismith James H JH
Nature chemical biology 20150622 8
Regioselective modification of amino acids within the context of a peptide is common to a number of biosynthetic pathways, and many of the resulting products have potential as therapeutics. The ATP-dependent enzyme LynD heterocyclizes multiple cysteine residues to thiazolines within a peptide substrate. The enzyme requires the substrate to have a conserved N-terminal leader for full activity. Catalysis is almost insensitive to immediately flanking residues in the substrate, suggesting that recog ...[more]