Elasticity coefficient

The rate of a chemical reaction is influenced by many different factors, such as temperature, pH, reactant and product concentrations and other effectors. The degree to which these factors change the reaction rate is described by the elasticity coefficient. This coefficient is defined as follows: The rate of a chemical reaction is influenced by many different factors, such as temperature, pH, reactant and product concentrations and other effectors. The degree to which these factors change the reaction rate is described by the elasticity coefficient. This coefficient is defined as follows: ε S v = ∂ v ∂ S S v = ∂ ln ⁡ v ∂ ln ⁡ S {displaystyle varepsilon _{S}^{v}={frac {partial v}{partial S}}{frac {S}{v}}={frac {partial ln v}{partial ln S}}} where v {displaystyle v} denotes the reaction rate and S {displaystyle S} denotes the substrate concentration. The partial derivative in the definition indicates that the elasticity is measured with respect to changes in a factor S while keeping all other factors constant. The most common factors include substrates, products and effectors. The scaling of the coefficient ensures that it is dimensionless and independent of the units used to measure the reaction rate and magnitude of the factor. The elasticity coefficient is an integral part of metabolic control analysis and was introduced in the early 1970s and possibly earlier by Henrik Kacser and Burns in Edinburgh and Heinrich and Rapoport in Berlin. The elasticity concept has also been described by other authors, most notably Savageau in Michigan and Clarke at Edmonton. In the late 1960s Michael Savageau developed an innovative approach called biochemical systems theory that uses power-law expansions to approximate the nonlinearities in biochemical kinetics. The theory is very similar to metabolic control analysis and has been very successfully and extensively used to study the properties of different feedback and other regulatory structures in cellular networks. The power-law expansions used in the analysis invoke coefficients called kinetic orders which are equivalent to the elasticity coefficients. Bruce Clarke in the early 1970s developed a sophisticated theory on analyzing the dynamic stability in chemical networks. As part of his analysis Clarke also introduced the notion of kinetic orders and a power-law approximation that was somewhat similar to Savageau's power-law expansions. Clarke's approach relied heavily on certain structural characteristics of networks, called extreme currents (also called elementary modes in biochemical systems). Clarke's kinetic orders are also equivalent to elasticities.