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Cooperative effect of fructose bisphosphate and glyceraldehyde-3-phosphate dehydrogenase on aldolase action
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry, Biochemistry.
1990 (English)In: Biochimica et Biophysica Acta, ISSN 0006-3002, Vol. 1037, no 3, 307-312 p.Article in journal (Refereed) Published
Abstract [en]

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 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.

Place, publisher, year, edition, pages
1990. Vol. 1037, no 3, 307-312 p.
Keyword [en]
Macromolecular interaction, Dynamism, Modulation, Glycolytic enzyme, Specificity
URN: urn:nbn:se:uu:diva-121165DOI: 10.1016/0167-4838(90)90030-JISI: A1990CR03100007PubMedID: 2106914OAI: oai:DiVA.org:uu-121165DiVA: diva2:343693
Available from: 2010-08-15 Created: 2010-03-18 Last updated: 2010-11-04Bibliographically approved

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