Expression of Functional Human Sialyltransferases ST3Gal1 and ST6Gal1 in Escherichia coli.

ABSTRACT: Sialyltransferases (STs) are disulfide-containing, type II transmembrane glycoproteins that catalyze the transfer of sialic acid to proteins and lipids and participate in the synthesis of the core structure oligosaccharides of human milk. Sialic acids are found at the outermost position of glycostructures, playing a key role in health and disease. Sialylation is also essential for the production of recombinant therapeutic proteins (RTPs). Despite their importance, availability of sialyltransferases is limited due to the low levels of stable, soluble and active protein produced in bacterial expression systems, which hampers biochemical and structural studies on these enzymes and restricts biotechnological applications. We report the successful expression of active human sialyltransferases S

SUBMITTER: Ortiz-Soto ME 

PROVIDER: S-EPMC4864186 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature