Interaction of enzymes involved in triosephosphate metabolism. Comparison of yeast and rabbit muscle cytoplasmic systems.

TitleInteraction of enzymes involved in triosephosphate metabolism. Comparison of yeast and rabbit muscle cytoplasmic systems.
Publication TypeJournal Article
Year of Publication1986
AuthorsTompa, P., J. Bär, and J. Batke
JournalEur J Biochem
Volume159
Issue1
Pagination117-24
Date Published1986 Aug 15
ISSN0014-2956
KeywordsAnimals, Cytoplasm, Fructose-Bisphosphate Aldolase, Fructosediphosphates, Glycerolphosphate Dehydrogenase, Muscles, NAD, Phosphofructokinase-1, Rabbits, Saccharomyces cerevisiae, Species Specificity, Spectrometry, Fluorescence, Sugar Phosphates
Abstract

The affinity of baker's yeast (Saccharomyces cerevisiae) fructose-1,6-bisphosphate aldolase towards the metabolically related enzymes phosphofructokinase and glyceraldehyde-3-phosphate dehydrogenase was tested by using a fluorescence-probe technique with fluorescein isothiocyanate attached covalently to the enzymes. The dissociation constants of the enzyme-enzyme complexes, as well as the rate constants of association and dissociation, were determined. Data were compared with the parameters derived from a mammalian (rabbit muscle) system, known from the literature and determined under the same conditions (pH 7.5 or 8.5 in 0.05 M Tris/HCl buffer at 20 degrees C). The comparison reveals similarities in the supramolecular organization of these cytoplasmic enzymes in phylogenetically distant species. Moreover, the fact that in vitro hybrid complexes are formed of stability comparable to that of non-hybrid complexes indicates that this ancient characteristic is probably conserved during evolution. A possible regulatory mechanism is presented, based on the dynamic competition, with each other, of the enzymes involved in triosephosphate metabolism.

Alternate JournalEur. J. Biochem.
PubMed ID2943591