Premium
Mechanism of the hydrolysis of adenosine 5′‐triphosphate: A regression analysis of kinetic data
Author(s) -
Hibbert D. Brynn,
Sandall John P. B.
Publication year - 1989
Publication title -
journal of chemometrics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.47
H-Index - 92
eISSN - 1099-128X
pISSN - 0886-9383
DOI - 10.1002/cem.1180030405
Subject(s) - adenosine , hydrolysis , pyrophosphate , atp hydrolysis , regression analysis , chemistry , kinetic energy , statistic , adenosine triphosphate , data set , rate equation , reaction rate constant , thermodynamics , mathematics , statistics , kinetics , physics , organic chemistry , biochemistry , atpase , quantum mechanics , enzyme
Data of the hydrolysis of adenosine 5′‐triphosphate have been re‐evaluated using a computer program that numerically integrates the differential rate equations within a routine that optimizes rate coefficients given a suitable model and concentration versus time data. The model is tested by calculation of Hamilton R ‐values, the Fisher F ‐statistic, a sensitivity analysis, the standard errors on the rate coefficients and by constructing contour maps of the objective function versus two rate coefficients. An optimization using only phosphate concentration data cannot distinguish between a model in which adenosine 5′‐monophosphate is formed predominantly directly with a molecule of pyrophosphate, and one in which it is formed via adenosine 5′‐diphosphate. A more accurate set of rate coefficients is calculated from existing data and the relative importance of the two paths determined.