1) It can be a useful tool for glycoengineering as it can catalyze multiple linkages: Glc/Gal(-O)Ser/Thr, Glc/Gal(-S)Cys and Glc/Gal(beta)Glc/Gal(-O/S)Ser/Thr/Cys.
Additional Information
1) EntS diglycosylates EC peptide (enterocin 96) in vitro with two hexoses at Ser33 residue. 2) EntS modifies ECS33C and ECS33T peptides at Cys33 and Thr33 residues, respectively, therefore displays O-glycosyltransferase activity as well as S-glycosyltransferase activity. 3) Site-directed mutagenesis (at multiple conserved sites including DXD motif) suggests that EntS utilises the single active site for both mono- and di-glycosyltransferase activities and DXD motif (DAD in this case) is a part of an active site. 4) EntS displays sequential dissociative mechanism for iterative di-glycosylation. 5) The stereochemistry of the terminal linkage catalysed by EntS has beta-configuration in di-glycosylated peptide and it does not require a secondary structure/N-terminal alpha-helix in peptide for glycosylation, as previously observed in case of SunS and ThuS.
