Enzymatic and structural properties of human glutamine:fructose-6-phosphate amidotransferase 2 (hGFAT2).

ABSTRACT: Glycoconjugates play a central role in several cellular processes, and alteration in their composition is associated with numerous human pathologies. Substrates for cellular glycosylation are synthesized in the hexosamine biosynthetic pathway, which is controlled by the glutamine:fructose-6-phosphate amidotransfera-se (GFAT). Human isoform 2 GFAT (hGFAT2) has been implicated in diabetes and cancer; however, there is no information about structural and enzymatic properties of this enzyme. Here, we report a successful expression and purification of a catalytically active recombinant hGFAT2 (rhGFAT2) in Escherichia coli cells fused or not to a HisTag at the C-terminal end. Our enzyme kinetics data suggest that hGFAT2 does not follow the expected ordered bi-bi mechanism, and performs the gluco

SUBMITTER: Oliveira IA 

PROVIDER: S-EPMC7948480 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature