Premium
Identification of enzymes acting on α‐glycated amino acids in Bacillus subtilis
Author(s) -
Wiame Elsa,
Duquenne Armelle,
Delpierre Ghislain,
Van Schaftingen Emile
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.10.049
Subject(s) - bacillus subtilis , biochemistry , enzyme , lysine , chemistry , escherichia coli , amino acid , fructose , amadori rearrangement , biology , glycation , bacteria , genetics , receptor , gene
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‐ε‐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‐ε‐lysine (6‐phosphate). These enzymes are therefore involved in the metabolism of α‐glycated amino acids.