Inhibition of transketolase by N-acetylimidazole.
Transketolase from baker's yeast is rapidly inactivated in the presence of N-acetylimidazole. According to kinetic data, acetylation of one amino acid residue of the protein per active site is sufficient for TK* inactivation. The holoenzyme is inhibited more slowly than is apotransketolase. The presence of a tyrosine residue in the enzyme's active site, essential for activity, is suggested.
Kuimov
A N
AN
A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Kovina
M V
MV
Kochetov
G A
GA
D000107:Acetylation; D001665:Binding Sites; D007093:Imidazoles / Q000494:pharmacology*; D007700:Kinetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D014174:Transketolase / Q000037:antagonists & inhibitors*; D014443:Tyrosine
D007093:Imidazoles; D014443:Tyrosine; D014174:Transketolase; C012160:N-acetylimidazole