1. Identification of enzymes acting on alpha-glycated amino acids in Bacillus subtilis.
- Author
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Wiame E, Duquenne A, Delpierre G, and Van Schaftingen E
- Subjects
- Amino Acid Sequence genetics, Bacterial Proteins chemistry, Bacterial Proteins genetics, Catalysis, Escherichia coli Proteins chemistry, Escherichia coli Proteins genetics, Escherichia coli Proteins metabolism, Fructosamine chemistry, Fructosamine metabolism, Fructose metabolism, Glycine chemistry, Glycine metabolism, Glycoproteins chemistry, Kinetics, Lysine chemistry, Lysine metabolism, Phosphorylation, Protein Binding, Amino Acids metabolism, Bacillus subtilis enzymology, Bacterial Proteins metabolism, Fructose analogs & derivatives, Glycine analogs & derivatives, Glycoproteins metabolism, Lysine analogs & derivatives
- 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.
- Published
- 2004
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