EC Number   |
General Information |
Reference |
|---|
   2.7.1.171 | metabolism |
despite its ability to reduce the glycation of intracellular islet proteins, fructosamine-3-kinase is neither required for the maintenance of beta-cell survival and function under control conditions nor involved in protection against beta-cell glucotoxicity |
707061 |
| 2.7.1.171 | metabolism |
starvation and diabetes do not change the level of expression of FN3K in different tissues, and no regulation of FN3K expression is observed in human fibroblasts treated with condition mimicking the diabetic state |
738073 |
| 2.7.1.171 | more |
no correlations of enzyme activity with age, sex, body weight, blood cholesterol, or plasma glucose in an oral glucose tolerance test are observed. Subjects whose parents or siblings had a stroke show lower FN3K activity |
738072 |
| 2.7.1.171 | more |
the strained disulfides in the dimeric Arabidosis thalina enzyme function as redox switches to reversibly regulate the activity and dimerization of FN3K. Critical role for the ATP-binding P-loop in the redox regulation of FN3Ks. HsFN3K, in which the P-loop Cys is conserved, is redox-regulated and displayed altered oligomerization when proliferating cells are exposed to acute oxidative stress. Structure-function analysis, overview |
762465 |
| 2.7.1.171 | more |
the strained disulfides in the dimeric Arabidosis thalina enzyme function as redox switches to reversibly regulate the activity and dimerization of FN3K. Critical role for the ATP-binding P-loop in the redox regulation of FN3Ks. The P-loop is stabilized in an extended conformation by a Cys-mediated disulfide bond connecting two chains to form a covalently linked dimer in which the reduction of disulfides results in AtFN3K activation. Structure-function analysis, overview |
762465 |
| 2.7.1.171 | physiological function |
advanced glycation end-products are key players in pathogenesis of long-term vascular diabetes complications, several enzymes such as fructosamine 3-kinase (FN3K) and glyoxalase I (GLO I) are crucial in preventing glycation processes |
739258 |
| 2.7.1.171 | physiological function |
CS-0777, a candidate compound for autoimmune diseases, becomes phosphorylated to an active metabolite, M1, by fructosamine 3-kinase (FN3K) and FN3K-related protein (FN3K-RP, EC 2.7.1.172), and (2R)-2-amino-2-methyl-4-(1-methyl)-5-[4-(4-methylphenyl)butanoyl]-1H-pyrrol-2-yl)butyl dihydrogen phosphate is reverted back to CS-0777 by alkaline phosphatase (ALP) in the body |
762516 |
| 2.7.1.171 | physiological function |
FN3K serves as a protein repair enzyme and also in the metabolism of endogenously produced free fructose-epsilon-lysine. Repairing lysine residues may be important to restore enzymatic activity, proteinprotein interaction or recognition sites for phosphorylation (which often comprise basic residues) or ubiquitinylation |
707426 |
| 2.7.1.171 | physiological function |
fructosamine 3 kinase is a deglycating enzyme, which may play a key role in reducing diabetes-induced organ damage by removing bound glucose from glycated proteins |
738074 |
| 2.7.1.171 | physiological function |
fructosamine 3-kinase (FN3K) is involved in protein deglycation FN3K phosphorylates fructosamines on the third carbon of their sugar moiety, making them unstable and causing them to detach from proteins, suggesting a protective role of this enzyme. FN3K is able to break down the second intermediate of the non-enzymatic glycation cascade by phosphorylating fructoselysine to a fructoselysine-3-phosphate. The variability in FN3K activity is associated with some polymorphisms in the FN3K gene, FN3K involvement in diabetes, overview. FN3K might act in concert with other molecular mechanisms and may impact on gene expression and activity of other enzymes involved in deglycation process |
738073 |
