Cooperative effect of fructose bisphosphate and glyceraldehyde-3-phosphate dehydrogenase on aldolase action

Jiri Neuzil, Helena Danielson, G. Rickey Welch, J. Ovádi

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

The combination of binding and kinetic approaches is suggested to study (i) the mechanism of substrate-modulated dynamic enzyme associations; (ii) the specificity of enzyme interactions. The effect of complex formation between aldolase and glyceraldehyde-3-phosphate dehydrogenase (d-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating), EC 1.2.1.12) on aldolase catalysis was investigated under pseudo-first-order conditions. No change in kcat but a significant increase in KM of fructose 1,6-bisphosphate for aldolase was found when both enzymes were obtained from muscle. In contrast, kcat rather than KM changed if dehydrogenase was isolated from yeast. Next, the conversion of fructose 1-phosphate was not affected by interactions between enzyme couples isolated from muscle. The influence of fructose phosphates on the enzyme-complex formation was studied by means of covalently attached fluorescent probe. We found that the interaction was not perturbed by the presence of fructose 1-phosphate; however, fructose 1,6-bisphosphate altered the dissociation constant of the enzyme complex. A molecular model for fructose 1,6-bisphosphate-modulated enzyme interaction has been evaluated which suggests that high levels of fructose bisphosphate would drive the formation of the 'channelling' complex between aldolase and glyceraldehyde-3-phosphate dehydrogenase.

Original languageEnglish
Pages (from-to)307-312
Number of pages6
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1037
Issue number3
DOIs
Publication statusPublished - Mar 1 1990

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Fructose-Bisphosphate Aldolase
Glyceraldehyde-3-Phosphate Dehydrogenases
Fructose
Enzymes
Muscle
Oxidoreductases
Glyceraldehyde 3-Phosphate
Muscles
Molecular Models
Catalysis
Fluorescent Dyes
NAD
Yeast
Yeasts
Phosphates
Kinetics
Substrates

Keywords

  • Dynamism
  • Glycolytic enzyme
  • Macromolecular interaction
  • Modulation
  • Specificity

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology

Cite this

Cooperative effect of fructose bisphosphate and glyceraldehyde-3-phosphate dehydrogenase on aldolase action. / Neuzil, Jiri; Danielson, Helena; Welch, G. Rickey; Ovádi, J.

In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 1037, No. 3, 01.03.1990, p. 307-312.

Research output: Contribution to journalArticle

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