Fructosamine 3-kinase, an enzyme involved in proteins deglycation
(2002)
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- (en) Fructosamines are formed from glucose and primary amines in a spontaneous, two-step reaction. When this reaction involves aminogroups of proteins, it is termed protein glycation. The formation of fructosamines is a slow and nearly irréversible process, and the extent of glycation of a protein in vivo is proportional to the blood glucose concentration. The measurement of glycated proteins is therefore considered to reflect the mean blood glucose level, and is used to monitor diabètes therapy. Once formed, fructosamines may spontaneously convert to a variety of compounds collectively called advanced glycation end-products, and which are believed to play a rôle in the development of the complications of diabètes. Fructose 3-phosphate is an intriguing phosphate ester that was discovered in 1990 by Szwergold and co-workers. It is formed from fructose in érythrocytes and lenses by an enzyme that displays a low affinity for this ketose. Furthermore, fructose 3-phosphate does not appear to be involved in any metabolic pathway. The working hypothesis of this thesis was therefore that the physiological function of “fructose 3-kinase” is to phosphorylate (a) compound(s) different from, yet structurally related to fructose, possibly fructosamines. The objectives were to test this hypothesis, purify and clone “fructose 3-kinase” and détermine its physiological function.
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Delpierre, G. (2002). Fructosamine 3-kinase, an enzyme involved in proteins deglycation. https://hdl.handle.net/2078.5/124226