Characterization of a metal-independent CAZy family 6 glycosyltransferase from Bacteroides ovatus.

ABSTRACT: The myriad functions of complex carbohydrates include modulating interactions between bacteria and their eukaryotic hosts. In humans and other vertebrates, variations in the activity of glycosyltransferases of CAZy family 6 generate antigenic variation between individuals and species that facilitates resistance to pathogens. The well characterized vertebrate glycosyltransferases of this family are multidomain membrane proteins with C-terminal catalytic domains. Genes for proteins homologous with their catalytic domains are found in at least nine species of anaerobic commensal bacteria and a cyanophage. Although the bacterial proteins are strikingly similar in sequence to the catalytic domains of their eukaryotic relatives, a metal-binding Asp-X-Asp sequence, present in a wide array of meta

SUBMITTER: Tumbale P 

PROVIDER: S-EPMC2757216 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature