Aldolase-catalysed inactivation of glyceraldehyde-3-phosphate dehydrogenase [26]

Research output: Contribution to journalArticle

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Abstract

ALDOLASE is known to catalyse its own inactivation in the presence of substrate and electron acceptors1. The underlying mechanism is that in the presence of electron acceptors aldolase catalyses the oxidation of dihydroxyacetone phosphate to hydroxypyruvaldehyde phosphate2,3 and this highly reactive nascent α-dicarbonyl reacts in situ with an active-centre residue4. Inactivation of aldolase is entirely due to reaction in situ of nascent hydroxypyruvaldehyde phosphate, for hydration and dilution of released hydroxypyruvaldehyde phosphate practically abolishes its contribution to inactivation4. As the inactivating agent loses reactivity on diffusion into solvent4, its action is restricted to the enzyme molecule that has produced it; other molecules of aldolase or other enzymes (transaldolase, transketolase) are not inactivated by aldolase-generated reagent1. We report here that oxidative cycles of aldolase cause the inactivation of glyceraldehyde-3-phosphate dehydrogenase (GAPD), suggesting a direct transfer of the inactivating agent between the two enzymes. Kinetic evidence for an interaction between aldolase and GAPD has been presented 5.

Original languageEnglish
Pages (from-to)94-95
Number of pages2
JournalNature
Volume276
Issue number5683
DOIs
Publication statusPublished - 1978

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Fructose-Bisphosphate Aldolase
Glyceraldehyde-3-Phosphate Dehydrogenases
Transaldolase
Enzymes
Dihydroxyacetone Phosphate
Transketolase
Electrons

ASJC Scopus subject areas

  • General

Cite this

Aldolase-catalysed inactivation of glyceraldehyde-3-phosphate dehydrogenase [26]. / Patthy, L.; Vas, M.

In: Nature, Vol. 276, No. 5683, 1978, p. 94-95.

Research output: Contribution to journalArticle

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abstract = "ALDOLASE is known to catalyse its own inactivation in the presence of substrate and electron acceptors1. The underlying mechanism is that in the presence of electron acceptors aldolase catalyses the oxidation of dihydroxyacetone phosphate to hydroxypyruvaldehyde phosphate2,3 and this highly reactive nascent α-dicarbonyl reacts in situ with an active-centre residue4. Inactivation of aldolase is entirely due to reaction in situ of nascent hydroxypyruvaldehyde phosphate, for hydration and dilution of released hydroxypyruvaldehyde phosphate practically abolishes its contribution to inactivation4. As the inactivating agent loses reactivity on diffusion into solvent4, its action is restricted to the enzyme molecule that has produced it; other molecules of aldolase or other enzymes (transaldolase, transketolase) are not inactivated by aldolase-generated reagent1. We report here that oxidative cycles of aldolase cause the inactivation of glyceraldehyde-3-phosphate dehydrogenase (GAPD), suggesting a direct transfer of the inactivating agent between the two enzymes. Kinetic evidence for an interaction between aldolase and GAPD has been presented 5.",
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N2 - ALDOLASE is known to catalyse its own inactivation in the presence of substrate and electron acceptors1. The underlying mechanism is that in the presence of electron acceptors aldolase catalyses the oxidation of dihydroxyacetone phosphate to hydroxypyruvaldehyde phosphate2,3 and this highly reactive nascent α-dicarbonyl reacts in situ with an active-centre residue4. Inactivation of aldolase is entirely due to reaction in situ of nascent hydroxypyruvaldehyde phosphate, for hydration and dilution of released hydroxypyruvaldehyde phosphate practically abolishes its contribution to inactivation4. As the inactivating agent loses reactivity on diffusion into solvent4, its action is restricted to the enzyme molecule that has produced it; other molecules of aldolase or other enzymes (transaldolase, transketolase) are not inactivated by aldolase-generated reagent1. We report here that oxidative cycles of aldolase cause the inactivation of glyceraldehyde-3-phosphate dehydrogenase (GAPD), suggesting a direct transfer of the inactivating agent between the two enzymes. Kinetic evidence for an interaction between aldolase and GAPD has been presented 5.

AB - ALDOLASE is known to catalyse its own inactivation in the presence of substrate and electron acceptors1. The underlying mechanism is that in the presence of electron acceptors aldolase catalyses the oxidation of dihydroxyacetone phosphate to hydroxypyruvaldehyde phosphate2,3 and this highly reactive nascent α-dicarbonyl reacts in situ with an active-centre residue4. Inactivation of aldolase is entirely due to reaction in situ of nascent hydroxypyruvaldehyde phosphate, for hydration and dilution of released hydroxypyruvaldehyde phosphate practically abolishes its contribution to inactivation4. As the inactivating agent loses reactivity on diffusion into solvent4, its action is restricted to the enzyme molecule that has produced it; other molecules of aldolase or other enzymes (transaldolase, transketolase) are not inactivated by aldolase-generated reagent1. We report here that oxidative cycles of aldolase cause the inactivation of glyceraldehyde-3-phosphate dehydrogenase (GAPD), suggesting a direct transfer of the inactivating agent between the two enzymes. Kinetic evidence for an interaction between aldolase and GAPD has been presented 5.

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