1996European Journal of BiochemistryRequires access

Transient‐State Kinetic Evidence Against a Channelled Transfer of Glyceraldehyde 3‐Phosphate from Aldolase to Glyceraldehyde‐3‐Phosphate Dehydrogenase

Wilma Martı́nez Arias, Gösta Pettersson

Open publisher page 3 citations

Abstract

Theoretical and experimental evidence is presented which leads to a rejection of the proposal that the transient‐state kinetics of the coupled two‐enzyme reaction involving aldolase and glyceraldehyde‐3‐phosphate dehydrogenase are indicative of a channelled transfer of glyceraldehyde 3‐phosphate from the producing enzyme to the consuming one.

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What this paper is about

Theoretical and experimental evidence is presented which leads to a rejection of the proposal that the transient‐state kinetics of the coupled two‐enzyme reaction involving aldolase and glyceraldehyde‐3‐phosphate dehydrogenase are indicative of a channelled transfer of glyceraldehyde 3‐phosphate from the producing enzyme to the consuming one.

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OpenAlex reports 3 citations for this work. Citation counts describe recorded attention and do not establish research quality.

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Available abstract

Theoretical and experimental evidence is presented which leads to a rejection of the proposal that the transient‐state kinetics of the coupled two‐enzyme reaction involving aldolase and glyceraldehyde‐3‐phosphate dehydrogenase are indicative of a channelled transfer of glyceraldehyde 3‐phosphate from the producing enzyme to the consuming one.

Key concepts: Aldolase A, Glyceraldehyde 3-phosphate dehydrogenase, Glyceraldehyde, Dehydrogenase, Aldolase B, Kinetics, Fructose-bisphosphate aldolase, Chemistry

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