PMID: 7011316Sep 1, 1980Paper

Analysis of progress curves. Rate law of pyruvate kinase type I from Escherichia coli

The Biochemical Journal
M MarkusM Malcovati

Abstract

Progress curves of the reaction catalysed by pyruvate kinase from Escherichia coli K12, designed to cover the four-dimensional concentration space of phosphoenolpyruvate, ADP, Mg2+ and ATP in the regulatory region, were recorded with the pH-stat method (pH 7.0 and 25 degrees C). Additional initial-rate measurement were performed to assess specific points. Two methods for the evaluation of progress curves were used: fitting the rate law to the rates obtained from the tangents of the progress curves and fitting the integrated rate law directly to the curves. Two models, both extensions of the concerted model given by Monod, Wyman & Changeux [(1965) J. Mol. Biol. 12, 88--118] with four protomers, could be fitted to the data within the experimental error. Model discrimination in favour of one of these models was possible by proper experimental design. In the selected model one conformational state of the enzyme forms the active complex. The active site of a second conformational state forms abortive complexes with Mg2+, causing strong inhibition at high Mg2+ concentrations. In the absence of ligands, most of the enzyme is in a third state that binds ATP at an allosteric site.

Citations

Sep 19, 2006·Analytical Biochemistry·Omar A Gutierrez, U Helena Danielson
Mar 7, 2012·PloS One·Ildefonso M De la Fuente, Jesus M Cortes
May 29, 2009·Journal of the Royal Society, Interface·Christoph Hold, Sven Panke
Oct 20, 2010·International Journal of Molecular Sciences·Ildefonso Martínez de la Fuente
Apr 25, 2000·Biochemical and Biophysical Research Communications·J C Diaz Ricci
Jun 1, 1985·Biophysical Chemistry·M MarkusB Hess
Jan 1, 1995·Bio Systems·I Martinez de la FuenteJ Veguillas
May 1, 1990·Molecular and Biochemical Parasitology·D BuckwitzC Gerth
Aug 1, 1988·Computers and Biomedical Research, an International Journal·V W SooL Garfinkel

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