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FEBS Lett. 2004 Nov 19;577(3):469-72.

Identification of enzymes acting on alpha-glycated amino acids in Bacillus subtilis.

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Laboratory of Physiological Chemistry, ICP and Université Catholique de Louvain, P.O. Box 7539, Avenue Hippocrate 75, B-1200 Brussels, Belgium.

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  • FEBS Lett. 2005 Jan 3;579(1):294.


We have characterized the Bacillus subtilis homologs of fructoselysine 6-kinase and fructoselysine-6-phosphate deglycase, two enzymes that specifically metabolize the Amadori compound fructose-epsilon-lysine in Escherichia coli. The B. subtilis enzymes also catalyzed the phosphorylation of fructosamines to fructosamine 6-phosphates (YurL) and the conversion of the latter to glucose 6-phosphate and a free amino acid (YurP). However, their specificity was totally different from that of the E. coli enzymes, since they acted on fructoseglycine, fructosevaline (YurL) or their 6-phosphoderivatives (YurP) with more than 30-fold higher catalytic efficiencies than on fructose-alpha-lysine (6-phosphate). These enzymes are therefore involved in the metabolism of alpha-glycated amino acids.

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