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Phenylanine can produce acetyl-coa and fumarate. How many ATPs can the catabolism of Phenylalanine produce? Please...

Phenylanine can produce acetyl-coa and fumarate. How many ATPs can the catabolism of Phenylalanine produce? Please explain how and from where those ATPs are coming from.

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The process of catabolism releases energy that can be used to produced ATP. The process of anabolism requires ATP, thus producing ADP at the end. However, catabolism requires the investment of ATP at the beginning (glycolysis), but at the end it results in a net gain.While the ATP count is glycolysis and the Krebs cycle is two ATP molecules, the electron transport chain contributes, at most, twenty-eight ATP molecules.

There are three stages in the catabolism.

Stage 1: Hydrolysis of macromolecules to subunits.

Stage 2: Conversion of subunits to form that can be completely oxidized to acetyl CoA.

Stage 3: Complete oxidization of Acetyl CoA and the production of A

Oxidative deamination is the first step to breaking down the amino acids so that they can be converted to sugars. The process begins by removing the amino group of the amino acids. The amino group becomes ammonium as it is lost and later undergoes the urea cycle to become urea, in the liver. It is then released into the blood stream, where it is transferred to the kidneys, which will secrete the urea as urine. The remaining portion of the amino acid becomes oxidized, resulting in an alpha-keto acid. The alpha-keto acid will then proceed into the TCA cycle, in order to produce energy. The acid can also enter glycolysis, where it will be eventually converted into pyruvate. The pyruvate is then converted into acetyl-CoA so that it can enter the TCA cycle and convert the original pyruvate molecules into ATP, or usable energy for the organism.

Transamination leads to the same end result as deamination: the remaining acid will undergo either glycolysis or the TCA cycle to produce energy that the organism's body will use for various purposes. This process transfers the amino group instead of losing the amino group to be converted into ammonium. The amino group is transferred to alpha-ketoglutarate, so that it can be converted to glutamate. Then glutamate transfers the amino group to oxaloacetate. This transfer is so that the oxaloacetate can be converted to aspartate or other amino acids. Eventually, this product will also proceed into oxidative deamination to once again produce alpha-ketoglutarate, an alpha-keto acid that will undergo the TCA cycle, and ammonium, which will eventually undergo the urea cycle.

Transaminases are enzymes that help catalyze the reactions that take place in transamination. They help catalyze the reaction at the point when the amino group is transferred from the original amino acid, like glutamate to alpha-ketoglutarate, and hold onto it to transfer it to another alpha-ketoacid.

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