PMID: 42270Jan 1, 1979

pH and temperature dependence of the double inhibition of D-glyceraldehyde-3-phosphate dehydrogenase by ATP and quinaldate

Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae
L V LienT Keleti

Abstract

ATP and quinaldate, two inhibitors of D-glyceraldehyde-3-phosphate dehydrogenase, act antagonistically if [Pi] greater than 1 mM, at pH 7.5 and 25 degrees C. However, the type of interaction of the two inhibitors changes with pH and temperature. Antagonism is strongest at pH values near neutrality and decreases at higher pH. Above pH 9.5 the two inhibitors act nearly additively. At pH 8.5 and [Pi] = 5 mM there is antagonism above 20 degrees C between the two inhibitors whereas there is synergy below 20 degrees C. A lag period in the time course of the enzyme reaction was detected when both inhibitors were present. The lag period is a function of pH. Below pH 8.5 the pH-dependence of the lag period resembles a titration curve with a pKapp greater than 8.

Related Concepts

GAPDH gene
Quinolines
Quinaldines
Muscle
Metabolic Inhibition
Glyceraldehyde-3-phosphate dehydrogenase
Glyceraldehyde-3-Phosphate Dehydrogenases
Titration Method
Hydrogen-Ion Concentration
Adenosine Triphosphate, Chromium Ammonium Salt

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