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Inhibition of transketolase by N-acetylimidazole.

A N Kuimov, Marina V. Kovina, G A Kochetov

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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.

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What this paper is about

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.

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Available 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.

Key concepts: Transketolase, Residue (chemistry), Chemistry, Tyrosine, Active site, Biochemistry, Acetylation, Enzyme

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