General description

Mammalian fructosamine-3-kinase (FN3K) catalyzes phosphorylation of fructosamines formed by glycation, the nonenzymatic reaction of glucose with primary amines. FN3K for example catalyzes transformation of fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate (FL3P). This phosphorylation destablilizes FL and propels spontaneous decomposition, thereby reversing at an early stage the nonenzymatic glycation process. Phosphorylation of fructosamines may initiate metabolism of the modified amine and result in deglycation of glycated proteins. In mammals, FN3K has a closely related homologue, FN3KRP (FN3K-related protein), which in the human genome is located just 8 kb upstream of FN3K on chromosome 17q25.3 FN3KRP, which is 68% sequence identity with FN3K, is a deglycating enzyme which phosphorylates the third carbon of the sugar moiety of ketosamines, and may play a role in freeing proteins from ribulosamines or psicosamines. A deglycation system may be an important factor in protecting cells from the deleterious effects of nonenzymatic glycation, which appears to be an important factor in the pathogenesis of diabetic complications.

Immunogen

FN3X (NP_078895, 284-319)
This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the C-terminal region of human FN3X.