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Literature summary extracted from

  • Avemaria, F.; Carrera, P.; Lapolla, A.; Sartore, G.; Chilelli, N.C.; Paleari, R.; Ambrosi, A.; Ferrari, M.; Mosca, A.
    Possible role of fructosamine 3-kinase genotyping for the management of diabetic patients (2015), Clin. Chem. Lab. Med., 53, 1315-1320.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.171 gene FN3K, located on chromosome 17q25.3, genotyping Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.171 additional information analysis of the FN3K gene on a Caucasian cohort of diabetic patients, molecular characterization of the FN3K gene by analyzing its promoter and of polymorphisms, c-385A/G (rs3859206) and the c-232A/T (rs2256339), associated with FN3K enzymatic activity in erythrocytes, as well as two variants c-421C/T and c-429delATCGGAG Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.171 deoxymorpholinofructose a competitive inhibitor Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.171 Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.171 ATP + [protein]-N6-D-fructosyl-L-lysine Homo sapiens
-
 ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.171 Homo sapiens Q9H479 gene FN3K
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.171 brain
-
 Homo sapiens
-
2.7.1.171 erythrocyte
-
 Homo sapiens
-
2.7.1.171 lens
-
 Homo sapiens
-
2.7.1.171 additional information FN3K is more active in tissues containing proteins with long (half-)lives, such as erythrocytes, lens and brain Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.171 ATP + [protein]-N6-D-fructosyl-L-lysine
-
 Homo sapiens ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
 ?
2.7.1.171 additional information the fructosamines bound to Lys139alpha, located near the C-terminus of the alpha subunits, and Lys16alpha, located on a loop of the alpha subunits, are good substrates. The N-terminal glycated valine is a poor substrate, consistent with free fructosevaline being a much poorer substrate than free fructoselysine Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.171 FN3K
-
 Homo sapiens
2.7.1.171 fructosamine 3-kinase
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.171 ATP
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
2.7.1.171 evolution the FN3K gene may have arisen by an event of duplication of an ancestral gene, FN3K-related protein (FN3K-RP). The gene encoding FN3K-RP is located next to the one encoding FN3K, and share a 65% sequence homology with FN3K and an identical genome organization. Both FN3K and FN3K-RP phosphorylate psicosamines and ribulosamines, but only the former act on fructosamines Homo sapiens
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 Homo sapiens
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 Homo sapiens