| Value |
-35.7
kJ/mol
Range: Table - link kJ/mol
|
| Organism |
Unspecified |
| Reference |
Thauer RK, Jungermann K, Decker K. Energy conservation in chemotrophic anaerobic bacteria.Bacteriol Rev. 1977 Mar41(1):100-80. p.108 table 4PubMed ID860983
|
| Primary Source |
[203] Guynn RW, Gelberg HJ, Veech RL. Equilibrium constants of the malate dehydrogenase, citrate synthase, citrate lyase, and acetyl coenzyme A hydrolysis reactions under physiological conditions. J Biol Chem. 1973 Oct 25 248(20):6957-65PubMed ID4743509
|
| Comments |
P.107 left column bottom paragraph: ""Energy-rich" compounds are characterized by their free energy of hydrolysis ("group transfer potential") (ΔG0'), which lies in the range of -5 to -15 kcal/mol (-20.9 to -62.8 kJ/mol) and by the fact that they exist in an enzymatic equilibrium with the ATP system. These "energy-rich" compounds are acid anhydrides or thioesters (Table 4), i.e., derivatives of carboxylic acids which represent the highest oxidation level of the carbon atom in organic compounds." Table gives gibbs free energies for hydrolysis of Energy-rich compounds involved in Substrate-level phosphorylation (SLP). SLP is a type of chemical reaction that results in the formation and creation of adenosine triphosphate (ATP) by the direct transfer and donation of a phosphate group to adenosine diphosphate (ADP) from a reactive intermediate. In cells, it occurs primarily and firstly in the cytoplasm (in glycolysis) under both aerobic and anaerobic conditions. Acetyl CoA enters the citric acid cycle and after 5 intermediates is converted into Succynil CoA which undergoes SLP |
| Entered by |
Uri M |
| ID |
104430 |