1. Identification of enzymes acting on α-glycated amino acids in Bacillus subtilis
- Author
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Wiame, Elsa, Duquenne, Armelle, Delpierre, Ghislain, and Van Schaftingen, Emile
- Subjects
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ENZYMES , *AMINO acids , *BACILLUS subtilis , *CATALYSTS - 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-#x03B5;-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-#x03B5;-lysine (6-phosphate). These enzymes are therefore involved in the metabolism of α-glycated amino acids. [Copyright &y& Elsevier]
- Published
- 2004
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