Irreversible inhibition of aldolase by a phosphorylated alpha-dicarbonyl compound.
The preparation of a phosphorylated alpha-dicarbonyl compound designed to specifically react with arginine residues of enzymes accepting phosphorylated compounds as effectors is reported, and shown to inhibit rabbit muscle aldolase in a time-dependent and irreversible manner. This irreversible inhibition occured in a buffer devoid of borate ions, suggesting that the presence of the phosphate moiety contributes in the stabilization of the adduct formed with arginine residues. Under the same conditions, the metalloenzyme iron superoxide dismutase, in which an arginine is known to be critical for the catalytic function, is not significantly inhibited.
Chabot
Nicolas
N
Groupe de Chimie Organique Biologique, Laboratoire LSPCMIB - UMR 5068 CNRS, Université Paul Sabatier, Toulouse cedex 9, France.
Vinatier
Virginie
V
Gefflaut
Thierry
T
Baudoin
Cecile
C
Rodriguez
Frederic
F
Blonski
Casimir
C
Hoffmann
Pascal
P
D000818:Animals; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D005634:Fructose-Bisphosphate Aldolase / Q000037:antagonists & inhibitors*; D054354:Iron Carbonyl Compounds / Q000494:pharmacology*; D007659:Ketones / Q000494:pharmacology; D007700:Kinetics; D007783:Lactones / Q000494:pharmacology; D010766:Phosphorylation; D011817:Rabbits; D013482:Superoxide Dismutase / Q000037:antagonists & inhibitors / Q000378:metabolism
D004791:Enzyme Inhibitors; D007659:Ketones; D007783:Lactones; C004773:diketene; D054354:Iron Carbonyl Compounds; D013482:Superoxide Dismutase; D005634:Fructose-Bisphosphate Aldolase