A novel approach to measure all rate constants in the simplest enzyme kinetics model

Li, Banghe; Li, Bo; Shen, Yuefeng

doi:10.1007/s10910-008-9460-x

Cited by 7 publications

(13 citation statements)

References 18 publications

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“…It is an essential point of our new method that the curve (19) approximates the real reaction process well. In [28], we use the tangent line to approximate the real reaction when the reaction is near its end. Fig.…”

Section: Numerical Experimentsmentioning

confidence: 99%

“…1 illustrates a case calculated by computers, which shows that the red curve, that is the approximation curve (19) proposed in this paper, is much better than the tangent line after the initial period. To show this more convincing, we do the same experiment as in [28] to compare these two methods.…”

Section: Numerical Experimentsmentioning

confidence: 99%

“…We set k 1 = 0.3, k 2 = 0.2, k −1 = 0.1 and (S 0 , E 0 ) = (20, 0.5), which are the same settings as in [28]. Then, (S(t), E(t)) can be calculated for t > 0.…”

Section: Numerical Experimentsmentioning

confidence: 99%

“…The motivation to yield this new relation comes from mathematical observation, that is, we observe that a curve formed by inflection points of some integral curves is more close to the real reaction process than the tangent line used in [28]. This new relation is an absolutely new discovery which former scientists never pay any attention to, and its value has not been recognized completely yet.…”

Section: Introductionmentioning

confidence: 96%

“…But these methods do require additional complicated equipments. Recently, we provided a new approach to measure all the rate constants without using any additional equipment other than those needed for measuring K M and V max [28]. It only provides one more relation among these constants, which actually is the tangent line of integral curves at the end of the reaction [28].…”

Section: Introductionmentioning

confidence: 99%

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An improved method to measure all rate constants in the simplest enzyme kinetics model

Shen

2011

J Math Chem

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Since Adrian Brown and Victor Henri's work, the simplest enzyme kinetics model, which contains only three rate constants k 1 , k 2 and k −1 in 1902, has been thoroughly explored in many directions. By using the Michaelis-Menten equation, K M and k 2 can be measured quickly. All the three rate constants can be derived by temperature jump method or transient state kinetics, but both methods need more complicated techniques and equipments. In our previous paper (Li et al. in J Math Chem 46:290-301, 2009), we gave a method to measure all the rate constants which does not require any additional equipment other than those needed for measuring K M and k 2 . Here, we propose a new one which needs no additional equipment either. This method is based on a study of inflection points of integral curves. Numerical results show that the new one is much better than the previous one in two aspects: near the end of the reaction, the new one gives more accurate estimation; during the quasi-steady state of the reaction, it also gives good estimations while the previous one can not. Hence, this method not only advances the estimation accuracy, but also has more choices for measuring.

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Section: Numerical Experimentsmentioning

confidence: 99%

Section: Numerical Experimentsmentioning

confidence: 99%

“…We set k 1 = 0.3, k 2 = 0.2, k −1 = 0.1 and (S 0 , E 0 ) = (20, 0.5), which are the same settings as in [28]. Then, (S(t), E(t)) can be calculated for t > 0.…”

Section: Numerical Experimentsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations