Ontology highlight
ABSTRACT:
SUBMITTER: Thibodeaux GN
PROVIDER: S-EPMC3475617 | biostudies-literature | 2012 Nov
REPOSITORIES: biostudies-literature
Thibodeaux Gabrielle N GN van der Donk Wilfred A WA
Chemical communications (Cambridge, England) 20121101 86
Phosphorylation is an abundant post-translational modification involved in a myriad of cell signaling pathways. Herein, we have engineered the class II lantipeptide synthetase ProcM to generate a variety of peptides containing O-phosphoserine (pSer) and O-phosphothreonine (pThr) residues, either in vitro or in vivo. ...[more]