期刊
FEBS LETTERS
卷 577, 期 3, 页码 469-472出版社
WILEY
DOI: 10.1016/j.febslet.2004.10.049
关键词
fructosamine; Amadori product; glycolysis; sugar kinase; sugar isomerase
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-c-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-E-lysine (6-phosphate). These enzymes are therefore involved in the metabolism of alpha-glycated amino acids. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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