Open AccessMechanism of O‐Specific Polysaccharide Biosynthesis in Salmonella Serogroups C 2 and C 3
Author(s) -
SHIBAEV Vladimir N.,
DRUZHININA Tatia.,
POPOVA Alla N.,
ROZHNOVA Sophia Sh.,
KILESSO Valentina A.
Publication year - 1979
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1979.tb04244.x
Subject(s) - chemistry , residue (chemistry) , biochemistry , uridine diphosphate glucose , pyrophosphate , polysaccharide , transferase , enzyme , uridine diphosphate , glycosyltransferase , glycosyl , uridine , galactosyltransferase , biosynthesis , galactose , guanosine , stereochemistry , rna , gene
Cell envelope and soluble glycosyl transferase preparations from Salmonella newport (sero‐group C 2 ) and Salmonella kentucky (serogroup C 3 ) were found to catalyze formation of polyprenyl pyrophosphate tetrasaccharides corresponding to the structure of the repeating unit of the main chain of O‐specific polysaccharides. Plant polyprenyl phosphate may serve as an exogenous sugar acceptor. Galactose residue is an initiator of a chain growth: transfer of galactosyl phosphate from uridine diphosphate galactose onto the acceptor is followed by two consecutive mannosyl transfers from guanosine diphosphate mannose and rhamnosyl transfer from thymidine diphosphate rhamnose. Uridine diphosphate glucose and polyprenyl phosphate are converted by the enzyme preparations into polyprenyl monophosphate glucose which may transfer a glucosyl residue onto the polyprenyl pyrophosphate oligosaccharides. The resulting pentasaccharide derivatives may be polymerised by enzymes present in cell envelope preparations. The significance of these results for the understanding of the mechanism of O‐specific polysaccharide biosynthesis is discussed.