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Identification of enzymes acting on alpha-glycated amino acids in Bacillus subtilis
- Source :
- FEBS Letters, Vol. 577, no. 3, p. 469-472 (2004)
- Publication Year :
- 2004
-
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.
Details
- Database :
- OAIster
- Journal :
- FEBS Letters, Vol. 577, no. 3, p. 469-472 (2004)
- Notes :
- English
- Publication Type :
- Electronic Resource
- Accession number :
- edsoai.on1130578797
- Document Type :
- Electronic Resource