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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence / genetics
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Amino Acids / metabolism*
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Bacillus subtilis / enzymology*
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Catalysis
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism
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Fructosamine / chemistry
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Fructosamine / metabolism
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Fructose / analogs & derivatives*
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Fructose / metabolism
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Glycine / analogs & derivatives*
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Glycine / chemistry
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Glycine / metabolism
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Glycoproteins / chemistry
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Glycoproteins / metabolism*
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Kinetics
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Lysine / analogs & derivatives*
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Lysine / chemistry
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Lysine / metabolism
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Phosphorylation
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Protein Binding
Substances
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Amino Acids
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Bacterial Proteins
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Escherichia coli Proteins
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Glycoproteins
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fructosyl-lysine
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Fructose
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Fructosamine
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fructosyl-glycine
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Lysine
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Glycine