A new regulatory principle for in vivo biochemistry: Pleiotropic low affinity regulation by the adenine nucleotides – Illustrated for the glycolytic enzymes of Saccharomyces cerevisiae. Issue 17 (12th July 2013)

• Record Type: Journal Article
• Authors: Mensonides, Femke I.C.; Bakker, Barbara M.; Cremazy, Frederic; Messiha, Hanan L.; Mendes, Pedro; Boogerd, Fred C.; Westerhoff, Hans V.
• Is Part Of: FEBS letters. Volume 587:Issue 17(2013)
• Page Start: 2860
• Page End: 2867
• Publication Date: 2013-07-12
• Subjects: 2PGA -- 2-phosphoglyceric acid -- 3PGA -- 3-phosphoglyceric acid -- ADH -- alcohol dehydrogenase (EC 1.1.1.1) -- ALD -- fructose 1, 6-bisphosphate aldolase (EC 4.1.2.13) -- ENO -- enolase (EC 4.2.1.11) -- EtOH -- ethanol -- F16BP -- fructose 1, 6-bisphosphate -- F26BP -- fructose 2, 6-bisphosphate -- F6P -- fructose 6-phosphate -- G3PDH -- glycerol 3-phosphate dehydrogenase (EC 1.1.1.8) -- G6P -- glucose 6-phosphate -- G6PDH -- glucose-6-phosphate dehydrogenase (EC 1.1.1.49) -- GAP -- glyceraldehyde 3-phosphate -- GAPDH -- glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) -- Glc -- glucose -- HXK -- hexokinase (EC 2.7.1.1) -- LDH -- lactate dehydrogenase (EC 1.1.1.27) -- PDC -- pyruvate decarboxylase (EC 4.1.1.1) -- PEP -- phosphoenolpyruvate -- PFK -- phosphofructokinase (EC 2.7.1.11) -- PGI -- phosphoglucose isomerase (EC 5.3.1.9) -- PGK -- 3-phosphoglycerate kinase (EC 2.7.2.3) -- PGM -- phosphoglycerate mutase (EC 5.4.2.1) -- PYK -- pyruvate kinase (EC 2.7.1.40) -- Pyr -- pyruvate -- TPI -- triosephosphate isomerase (EC 5.3.1.1) -- Systems Biology -- Enzyme kinetics -- Energetics -- ATP -- Yeast glycolysis model; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.07.013
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : 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.