Halogenated pyruvate derivatives as substrates of transketolase from Saccharomyces cerevisiae

Olga A. Esakova, L. E. Meshalkina, G. A. Kochetov, R. Golbik

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Pyruvate derivatives halogenated at C3 were shown to be donor substrates in the transketolase reaction. No drastic differences between the derivatives were observed in the value of the catalytic constant, whereas the Michaelis constant increased in the following order: Br-pyruvate < Cl-pyruvate < Cl 2-pyruvate < F-pyruvate < Br2-pyruvate. The presence of the halogenated pyruvate derivatives increased the affinity of apotransketolase for the coenzyme; of note, the extent of this effect was equal with both of the active centers of the enzyme. In contrast, the presence of any other substrate known to date, including hydroxypyruvate (i.e. pyruvate hydroxylated at C3), induced nonequivalence of the active centers in that they differed in the extent to which the affinity for the coenzyme increased. Consequently, the β-hydroxyl of dihydroxyethylthiamine diphosphate (an intermediate of the transketolase reaction) played an important role in the phenomenon of non-equivalence of the active centers associated with the coenzyme binding. The fundamental possibility was demonstrated of using halogenated pyruvate derivatives as donors of the halogen-hydroxyethyl group in organic synthesis of halogenated carbohydrates involving transketolase.

Original languageEnglish (US)
Pages (from-to)1234-1238
Number of pages5
JournalBiochemistry (Moscow)
Volume74
Issue number11
DOIs
StatePublished - Nov 1 2009

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Transketolase
Pyruvic Acid
Yeast
Saccharomyces cerevisiae
Derivatives
Substrates
Coenzymes
Synthetic Chemistry Techniques
Halogens
Diphosphates
Hydroxyl Radical
Carbohydrates

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Esakova, Olga A. ; Meshalkina, L. E. ; Kochetov, G. A. ; Golbik, R. / Halogenated pyruvate derivatives as substrates of transketolase from Saccharomyces cerevisiae. In: Biochemistry (Moscow). 2009 ; Vol. 74, No. 11. pp. 1234-1238.
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abstract = "Pyruvate derivatives halogenated at C3 were shown to be donor substrates in the transketolase reaction. No drastic differences between the derivatives were observed in the value of the catalytic constant, whereas the Michaelis constant increased in the following order: Br-pyruvate < Cl-pyruvate < Cl 2-pyruvate < F-pyruvate < Br2-pyruvate. The presence of the halogenated pyruvate derivatives increased the affinity of apotransketolase for the coenzyme; of note, the extent of this effect was equal with both of the active centers of the enzyme. In contrast, the presence of any other substrate known to date, including hydroxypyruvate (i.e. pyruvate hydroxylated at C3), induced nonequivalence of the active centers in that they differed in the extent to which the affinity for the coenzyme increased. Consequently, the β-hydroxyl of dihydroxyethylthiamine diphosphate (an intermediate of the transketolase reaction) played an important role in the phenomenon of non-equivalence of the active centers associated with the coenzyme binding. The fundamental possibility was demonstrated of using halogenated pyruvate derivatives as donors of the halogen-hydroxyethyl group in organic synthesis of halogenated carbohydrates involving transketolase.",
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Halogenated pyruvate derivatives as substrates of transketolase from Saccharomyces cerevisiae. / Esakova, Olga A.; Meshalkina, L. E.; Kochetov, G. A.; Golbik, R.

In: Biochemistry (Moscow), Vol. 74, No. 11, 01.11.2009, p. 1234-1238.

Research output: Contribution to journalArticle

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AB - Pyruvate derivatives halogenated at C3 were shown to be donor substrates in the transketolase reaction. No drastic differences between the derivatives were observed in the value of the catalytic constant, whereas the Michaelis constant increased in the following order: Br-pyruvate < Cl-pyruvate < Cl 2-pyruvate < F-pyruvate < Br2-pyruvate. The presence of the halogenated pyruvate derivatives increased the affinity of apotransketolase for the coenzyme; of note, the extent of this effect was equal with both of the active centers of the enzyme. In contrast, the presence of any other substrate known to date, including hydroxypyruvate (i.e. pyruvate hydroxylated at C3), induced nonequivalence of the active centers in that they differed in the extent to which the affinity for the coenzyme increased. Consequently, the β-hydroxyl of dihydroxyethylthiamine diphosphate (an intermediate of the transketolase reaction) played an important role in the phenomenon of non-equivalence of the active centers associated with the coenzyme binding. The fundamental possibility was demonstrated of using halogenated pyruvate derivatives as donors of the halogen-hydroxyethyl group in organic synthesis of halogenated carbohydrates involving transketolase.

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