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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Wiame E,Duquenne A,Delpierre G,Van Schaftingen Edoi
10.1016/j.febslet.2004.10.049keywords:
subject
Has Abstractpub_date
2004-11-19 00:00:00pages
469-72issue
3eissn
0014-5793issn
1873-3468pii
S0014579304013018journal_volume
577pub_type
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