Phosphates, high-energy

PhenylPhosphorothioa.te Esters. These are the most widely used OP iasecticides and iacorporate pseudoanhydride high energy phosphate bonds between phosphoric acid and phenols that are present ia the activated P=0 state. 

Two and twelve moles of ATP are produced, respectively, per mole of glucose consumed in the glycolytic pathway and each turn of the Krebs (citrate) cycle. In fat metaboHsm, many high energy bonds are produced per mole of fatty ester oxidized. Eor example, 129 high energy phosphate bonds are produced per mole of palmitate. Oxidative phosphorylation has a remarkable 75% efficiency. Three moles of ATP are utilized per transfer of two electrons, compared to the theoretical four. The process occurs via a series of reactions involving flavoproteins, quinones such as coenzyme Q, and cytochromes. 

Hydrolases represent a significant class of therapeutic enzymes [Enzyme Commission (EC) 3.1—3.11] (14) (Table 1). Another group of enzymes with pharmacological uses has budt-ia cofactors, eg, in the form of pyridoxal phosphate, flavin nucleotides, or zinc (15). The synthases, and other multisubstrate enzymes that require high energy phosphates, are seldom available for use as dmgs because the required co-substrates are either absent from the extracellular space or are present ia prohibitively low coaceatratioas. 

Mitochondria Mitochondria are organelles surrounded by two membranes that differ markedly in their protein and lipid composition. The inner membrane and its interior volume, the matrix, contain many important enzymes of energy metabolism. Mitochondria are about the size of bacteria, 1 fim. Cells contain hundreds of mitochondria, which collectively occupy about one-fifth of the cell volume. Mitochondria are the power plants of eukaryotic cells where carbohydrates, fats, and amino acids are oxidized to CO9 and H9O. The energy released is trapped as high-energy phosphate bonds in ATR... 

Similarly, the release of free energy that occurs upon the hydrolysis of ATP and other high-energy phosphates can be treated quantitatively in terms of group transfer. It is common to write for the hydrolysis of ATP... 

So far, as in Equation (3.33), the hydrolyses of ATP and other high-energy phosphates have been portrayed as simple processes. The situation in a real biological system is far more complex, owing to the operation of several ionic equilibria. First, ATP, ADP, and the other species in Table 3.3 can exist in several different ionization states that must be accounted for in any quantitative analysis. Second, phosphate compounds bind a variety of divalent and monovalent cations with substantial affinity, and the various metal complexes must also be considered in such analyses. Consideration of these special cases makes the quantitative analysis far more realistic. The importance of these multiple equilibria in group transfer reactions is illustrated for the hydrolysis of ATP, but the principles and methods presented are general and can be applied to any similar hydrolysis reaction. 

Based on the discussion of high-energy phosphates in this chapter, would you expect carbamoyl phosphate to possess a high free energy of hydrolysis Provide a chemical rationale for your answer. 

The transport of each COg requires the expenditure of two high-energy phosphate bonds. The energy of these bonds is expended in the phosphorylation of pyruvate to PEP (phosphoenolpyruvate) by the plant enzyme pyruvate-Pj dikinase the products are PEP, AMP, and pyrophosphate (PPi). This represents a unique phosphotransferase reaction in that both the /3- and y-phosphates of a single ATP are used to phosphorylate the two substrates, pyruvate and Pj. The reaction mechanism involves an enzyme phosphohistidine intermediate. The y-phosphate of ATP is transferred to Pj, whereas formation of E-His-P occurs by addition of the /3-phosphate from ATP ... 

Suggest an explanation for the exergonic nature of the glycogen synthase reaction (AG° = - 13.3 kj/mol). Consult Chapter 3 to review the energetics of high-energy phosphate compounds if necessary. 

HIGH-ENERGY PHOSPHATES PLAY A CENTRAL ROLE IN ENERGY CAPTURE AND TRANSFER... 

HIGH-ENERGY PHOSPHATES ACT AS THE "ENERGY CURRENCY" OF THE CELL... 

Figure 10-5. StructureofATP, ADP, and AMP showing the position and the number of high-energy phosphates (- ).

Figure 10-6. Roie of ATP/ADP cycie in transfer of high-energy phosphate.

Figure 10-7. Transfer of high-energy phosphate between ATP and creatine.

Other Nucleoside Triphosphates Participate in the Transfer of High-Energy Phosphate... 

The Creatine Phosphate Shuttle Facilitates Transport of High-Energy Phosphate From Mitochondria... 

Figure 12-14. The creatine phosphate shuttle of heart and skeletal muscle. The shuttle allows rapid transport of high-energy phosphate from the mitochondrial matrix into the cytosol. CKg, creatine kinase concerned with large requirements for ATP, eg, muscular contraction CIC, creatine kinase for maintaining equilibrium between creatine and creatine phosphate and ATP/ADP CKg, creatine kinase coupling glycolysis to creatine phosphate synthesis CK, , mitochondrial creatine kinase mediating creatine phosphate production from ATP formed in oxidative phosphorylation P, pore protein in outer mitochondrial membrane.

Table 17-1. Generation of high-energy phosphate in the catabolism of glucose.

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