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This bond is also referred to as a high-energy phosphate bond.
Living systems store their energy in the cells as specific high-energy phosphate bonds linked to molecules similar to those used to build up the genes.
High-energy phosphate can mean one of two things:
Often, high-energy phosphate bonds are denoted by the character ' '.
Sometimes the "high-energy phosphate bond" of ATP is used to explain how this reaction produces energy.
For a protein containing n amino acids, the number of high-energy phosphate bonds required to translate it is 4n-1 .
Thus, high-energy phosphate reactions can:
The loss of a high-energy phosphate bond and the substrate for the rest of glycolysis makes formation of methylglyoxal inefficient.
The phosphagens are energy storage compounds, also known as high-energy phosphate compounds, are chiefly found in muscular tissue in animals.
When people speak of a high-energy phosphate pool, they speak of the total concentration of these compounds with these high-energy bonds.
High-energy phosphate bonds are pyrophosphate bonds, acid anhydride linkages formed by taking phosphoric acid derivatives and dehydrating them.
This step uses 2 "ATP equivalents" because pyrophosphate is cleaved into 2 molecules of inorganic phosphate, breaking a high-energy phosphate bond.
Two high-energy phosphate bonds (phosphoanhydride bonds) (those that connect adjacent phosphates) in an ATP molecule are responsible for the high energy content of this molecule.
Adenosine is formed in the myocardial cells during hypoxia, ischemia, or vigorous work, due to the breakdown of high-energy phosphate compounds (e.g., adenosine monophosphate, AMP).
Phosphocreatine is stored as a readily available high-energy phosphate supply, and the enzyme creatine phosphokinase transfers a phosphate from phosphocreatine to ADP to produce ATP.
ATP is generated in a following separate step (key difference from oxidative phosphorylation) by transfer of the high-energy phosphate on 1,3-bisphosphoglycerate to ADP via the enzyme phosphoglycerate kinase, generating 3-phosphoglycerate.
They allow a high-energy phosphate pool to be maintained in a concentration range, which, if it all were ATP, would create problems due to the ATP consuming reactions in these tissues.
The formation of this bond is quite thermodynamically unfavorable; even though PEP is a very high-energy phosphate compound, the equilibrium in PEP-PPR interconversion still favors PEP.
Additionally, the optimal production of the 12 biosynthetic precursors, high-energy phosphate bonds, and redox potential was calculated for each in silico deletion strain (Table 1) to determine the specific effect of the gene deletion on the metabolic capabilities.
Phosphocreatine, also known as creatine phosphate (CP) or PCr (Pcr), is a phosphorylated creatine molecule that serves as a rapidly mobilizable reserve of high-energy phosphates in skeletal muscle and the brain.
As muscle tissues can have sudden demands for lots of energy; these compounds can maintain a reserve of high-energy phosphates that can be used as needed, to provide the energy that could not be immediately supplied by glycolysis or oxidative phosphorylation.
From the standpoint of high energy phosphate accounting, the hydrolysis of ATP to AMP and PP requires two high-energy phosphates, as to reconstitute AMP into ATP requires two phosphorylation reactions.
However, the eno -and gpmAB - in silico deletion strains were limited in their production capability of high-energy phosphate bonds under all conditions, and were unable to produce any of the biosynthetic precursors in phase 6 even with the serine degradation pathway.
The in silico nuo -and cyoABCD -deletion strains were limited in their production capabilities of high-energy phosphate bonds for aerobic growth; however, under anaerobic conditions high-energy phosphate bonds were produced by substrate level phosphorylation.
At least four high-energy phosphate bonds are split to make each new peptide bond: two are consumed in charging a tRNA molecule with an amino acid (see Figure 6-56), and two more drive steps in the cycle of reactions occurring on the ribosome during synthesis itself (see Figure 6-66).