Identification of enzymes acting on alpha-glycated amino acids in Bacillus subtilis.

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 Lett

journal_title

FEBS letters

authors

Wiame E,Duquenne A,Delpierre G,Van Schaftingen E

doi

10.1016/j.febslet.2004.10.049

keywords:

subject

Has Abstract

pub_date

2004-11-19 00:00:00

pages

469-72

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014579304013018

journal_volume

577

pub_type

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