title: Inhibition of transketolase by N-acetylimidazole.
abstract: 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.
authors.affiliation: A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
authors.forename: A N
authors.initials: AN
authors.lastname: Kuimov
authors.forename: M V
authors.initials: MV
authors.lastname: Kovina
authors.forename: G A
authors.initials: GA
authors.lastname: Kochetov
mesh_terms: D000107:Acetylation; D001665:Binding Sites; D007093:Imidazoles / Q000494:pharmacology*; D007700:Kinetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D014174:Transketolase / Q000037:antagonists & inhibitors*; D014443:Tyrosine
chemical_list: D007093:Imidazoles; D014443:Tyrosine; D014174:Transketolase; C012160:N-acetylimidazole