Identification of enzymes acting on alpha-glycated amino acids in Bacillus subtilis
(2004) FEBS Letters — Vol. 577, n° 3, p. 469-472 (2004)
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- Abstract
- 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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Wiame, E., Duquenne, A., Delpierre, G., & Van Schaftingen, E. (2004). Identification of enzymes acting on alpha-glycated amino acids in Bacillus subtilis. FEBS Letters, 577(3), 469-472. https://doi.org/10.1016/j.febslet.2004.10.049 (Original work published 2004)