v5.1.0.3
Glycine data from LIS
Type | Family |
Description | This entry represents several alpha-2,3-sialyltransferase ( ) proteins, most of which are found in the food-borne pathogen Campylobacter jejuni. Sialyltransferases transfer a sialic acid moiety from cytidine-5'-monophospho-N-acetyl-neuraminic acid (CMP-NeuAc) to terminal positions of various key glycoconjugates, which play critical roles in cell recognition and adherence [ ]. The structure of Cst-II alpha-2,3-sialyltransferase from C. jejuni consists of a 3-layer alpha/beta/alpha topology. Cst-II catalytic mechanism involves an essential histidine (general base) and two tyrosine residues (coordination of the phosphate leaving group) to carry out substrate binding and glycosyl transfer. |
Short Name | A-2_3-sialyltransferase |