| Enzyme | Thermodynamics of Enzyme-Catalyzed Reactions | NIST |
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Thermodynamics of Enzyme-Catalyzed Reactions |
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Result pages :
| comments |
| For deuterated malate in the above reaction and under the same conditions given here, K' = 8.90E-4. |
| The result given here was calculated from the concentrations given in Pestlin et al.'s Table V. In this study, the position of equilibrium was not approached from both direction. Pestlin et al. also report additional data for reactions where the exact identity of the products is uncertain. |
| This result was also given in [61ATK/JOH]. |
| The apparent equilibrium constant given here was calculated from the concentrations given in Meyerhoff and Green's Table VII. |
| Talalay reports K'c(H+)/co = 2.11E-9 at an unspecified pH which we assume to be ~ 7.0. The apparent equilibrium constant given here is based on this result. Few details on the equilibrium measurements were given. |
| Brattlie carried out this reaction in two different buffers and with semicarbazide added to the reaction mixture. The result given here is the average of the results which have been corrected for the enthalpy of reaction of the acetaldehyde with the semicarbazide and for the enthalpies of protonation of the buffers. |
| From kinetic results, Crabb et al. found that 1.50E-11 < {K'c(H+)/co} < 2.18E-11. The result for K' was calculated from this result. |
| The apparent equilibrium constants given here were calculated from results given in Tomkin's Table IV. The temperature is assumed to be 298.15 K. |
| Eriksson reports K'c(H+)/co = 1.42E-9. This is approximately equal to K for the chemical reference reaction: trans-2-hexene-1-ol(aq) + NAD-(aq) = trans-2-hexanal(aq) + NADH2-(aq) + H+(aq). The apparent equilibrium constant given here was calculated from this result. |
| The apparent equilibrium constant given here was calculated from the result given in Table 2 in this paper. |
| Tewari and Goldberg also calculated K = (9.010.8)E-10 and ?rHo = (21.310.3) kJ mol-1 at T = 298.15 K and I = 0 for the reference reaction: D-sorbitol(aq) + NAD-(aq) = D-fructose(aq) + NADH2-(aq) + H+(aq). |
| Few details were given in this Proceedings abstract. |
| This result was attributed by Williamson et al. to R. L. Veech. |
| Stern reports K'c(H+)/co = 2.17E-10 at pH = 9.6. The apparent equilibrium constant given here was calculated from this result. Few details on the equilibrium investigation are reported. |
| The result given here is the unpublished result of Krebs and Stubbs. Few details were given. |
| George et al. reported ?rHo (Ic < 0.01 mol dm-3) = -2.5 kJ mol-1 for this chemical reference reaction. They did not report the calorimetric enthalpy of reaction or the conditions of measurement. |
| The apparent equilibrium constant given here was calculated from the concentrations given in Dayan and Wilson's Table II. |
| Wiesinger and Hinz reported ?rH(cal) = -54.0 kJ mol-1 for this biochemical reaction. However, the reported value included a correction for the hydration of the aldehyde form of D-glyceraldehyde 3-phosphate to its diol form. In the absence of these corrections, the value of ?rH(cal) for this reaction is -33.8 kJ mol-1 (H. Wiesinger, personal communication cited by Kishore et al. [98KIS/TEW]). This entry supersedes the entry made in Goldberg and Tewari's [95GOL/TEW] earlier review. |
| This reaction is catalyzed by the _2 subunit of tryptophan synthase. |
| Cook et al. report K'c(H+)/co = 2.9E-12 at pH = 9.0. The apparent equilibrium constant given here was calculated from this result. |
| Brattlie carried out this reaction in three different buffers and with semicarbazide added to the reaction mixture. The result given here is the average of the results which have been corrected for the enthalpy of reaction of the acetaldehyde with the semicarbazide and for the enthalpies of protonation of the buffers. |
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