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1 tivity relevant to Ni(II)-containing E. coli glyoxalase I.
2 planation for the stereochemical behavior of glyoxalase I.
3 ve inhibitor of the anticancer target enzyme glyoxalase I.
4 inhibit the methylglyoxal-detoxifying enzyme glyoxalase I.
5 ate that forms along the reaction pathway of glyoxalase I.
6 C is diminished in the absence of functional glyoxalase I.
7 ay for MG in E. coli and that the product of glyoxalase I activity, S-lactoylglutathione, is the acti
11 ncient betaalphabetabetabeta fold motif with glyoxalase I and bleomycin resistance protein families,
12 is of published values for the activities of glyoxalase I and glyoxalase II in lysed erythrocytes and
15 ied proteins, whereas other targets, such as glyoxalase I and ribose 5-phosphate isomerase, detoxify
16 elated to at least two other metalloenzymes, glyoxalase I and the Mn2+- or Fe2+-containing extradiol
17 The structure of the active site of human glyoxalase I and the reaction mechanism of the enzyme-ca
19 strains contained the glutathione-dependent glyoxalases I and II, as well as the glutathione-indepen
21 ites of human, yeast, and Pseudomonas putida glyoxalase I, as the log K(i) values for these mechanism
22 llographic measurements, indicate that human glyoxalase I binds the syn-conformer of S-(N-aryl-N-hydr
27 s that are catalyzed include isomerizations (glyoxalase I), epimerizations (methylmalonyl-CoA epimera
29 um-1,2-diolate) , we observed both decreased glyoxalase I expression and activity relative to untreat
30 nct superfamily of metalloenzymes containing glyoxalase I, extradiol dioxygenases, and methylmalonyl-
32 on is performed by a trypanothione-dependent glyoxalase I (GLO1) containing a nickel cofactor; all ot
33 say of MGS by coupling of the MG produced to glyoxalase I (Glx I): MG + glutathione (GSH) --> (S)-lac
42 the role of MGO and its metabolizing enzyme, glyoxalase I, in high glucose-induced apoptosis (annexin
44 se in the intracellular concentration of the glyoxalase I inhibitor (kapp = 1.41 +/- 0.03 min-1 (37 d
45 thylglyoxal metabolism with a cell permeable glyoxalase I inhibitor provoked these responses in normo
46 (N-aryl-N-hydroxycarbamoyl)glutathione-based glyoxalase I inhibitors culminated in the discovery of t
49 data suggest that the glutathione-dependent glyoxalase I is the dominant detoxification pathway for
53 hibition is due to competitive inhibition of glyoxalase I, preincubation of L1210 cells with 2(Et)2 i
54 on-dependent kinetic properties of the yeast glyoxalase I reaction have been measured by means of vis
58 lopentyl diester, a competitive inhibitor of glyoxalase I, resulted in apoptosis along with a dramati
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