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A new regulatory principle for in vivo biochemistry: pleiotropic low affinity regulation by the adenine nucleotides--illustrated for the glycolytic enzymes of Saccharomyces cerevisiae.

Authors
  • Mensonides, Femke I C1
  • Bakker, Barbara M
  • Cremazy, Frederic
  • Messiha, Hanan L
  • Mendes, Pedro
  • Boogerd, Fred C
  • Westerhoff, Hans V
  • 1 Department of Molecular Cell Physiology, Faculty of Earth and Life Sciences, VU University Amsterdam, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands. , (Netherlands)
Type
Published Article
Journal
FEBS letters
Publication Date
Sep 02, 2013
Volume
587
Issue
17
Pages
2860–2867
Identifiers
DOI: 10.1016/j.febslet.2013.07.013
PMID: 23856461
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Enzymology tends to focus on highly specific effects of substrates, allosteric modifiers, and products occurring at low concentrations, because these are most informative about the enzyme's catalytic mechanism. We hypothesized that at relatively high in vivo concentrations, important molecular monitors of the state of living cells, such as ATP, affect multiple enzymes of the former and that these interactions have gone unnoticed in enzymology. We test this hypothesis in terms of the effect that ATP, ADP, and AMP might have on the major free-energy delivering pathway of the yeast Saccharomyces cerevisiae. Assaying cell-free extracts, we collected a comprehensive set of quantitative kinetic data concerning the enzymes of the glycolytic and the ethanol fermentation pathways. We determined systematically the extent to which the enzyme activities depend on the concentrations of the adenine nucleotides. We found that the effects of the adenine nucleotides on enzymes catalysing reactions in which they are not directly involved as substrate or product, are substantial. This includes effects on the Michaelis-Menten constants, adding new perspective on these, 100 years after their introduction. Copyright © 2013. Published by Elsevier B.V.

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