Identification of enzymes acting on α‐glycated amino acids in Bacillus subtilis
- 30 October 2004
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 577 (3) , 469-472
- https://doi.org/10.1016/j.febslet.2004.10.049
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-ε-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-ε-lysine (6-phosphate). These enzymes are therefore involved in the metabolism of α-glycated amino acidsKeywords
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