FN3K phosphorylates ketosamines

Stable Identifier
Reaction [transition]
Homo sapiens
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Proteins can undergo chemical modifications such as glycation, which occurs when glucose and other free aldoses spontaneously react with N-terminal and eta-amino groups of proteins to form Schiff bases, which slowly rearrange to ketosamines or, if the sugar is glucose, fructosamines. Fructosamines can further react slowly and become advanced glycation end products, which are thought to play a role in the pathophysiology of several disorders, especially diabetic complications. Ketosamine-3-kinase (FN3K) and ketosamine-3-kinase-related protein (FN3KRP) can phosphorylate protein-bound or free ketosamines on the third carbon of the sugar moiety and the resultant, unstable ketosamine 3-phosphates decompose under physiological conditions (a process called deglycation). Both enzymes can 3-phosphorylate psicosamines (PsiAm) and ribulosamines (RibAm), but only FN3K can 3-phosphorylate fructosamines (FruAm) as well (Delpierre et al. 2000, 2004).
Literature References
PubMed ID Title Journal Year
15102834 Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin

Delpierre, G, Vertommen, D, Van Schaftingen, E, Rider, MH, Communi, D

J. Biol. Chem. 2004
11016445 Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase

Stroobant, V, Delpierre, G, Santos, H, Vanstapel, F, Van Schaftingen, E, Collard, F, Rider, MH

Diabetes 2000
Catalyst Activity

kinase activity of FN3K [cytosol]

Orthologous Events
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