AAs are not stored by the body and are present in cells, blood, and the extracellular fluids.
AAs must be acquired from the diet (essential amino acids), de novo synthesis (nonessential amino acids), and protein degradation.
AAs are depleted through body protein synthesis, biosynthesis of essential nitrogen-containing small molecules, and catabolism to glucose, glycogen, fatty acids, ketone bodies, or CO2 + H2O.
In the glucogenic pathway, aspartate and asparagine are converted to oxaloacetate.
Succinyl CoA is produced in the major glucogenic pathway and is converted to CoA via glycine.
In the degradation of aspartate, the major product is oxaloacetate.
In the degradation of aspartate, the minor product is fumarate.
In the glucogenic pathway, phenylalanine and tyrosine are converted to fumarate.
In the fed state, amino acids are used for the synthesis of proteins in the liver and in other tissues, with the excess used to produce glucose or triacylglycerol.
In the fasting state, muscle protein is cleaved to amino acids, with some of the amino acids oxidized to produce energy.
Phenylalanine and tyrosine are amino acids that yield fumarate in the ketogenic pathway.
Aspartate and asparagine are amino acids that yield OAA in the ketogenic pathway.
Protein turnover results from the simultaneous synthesis and degradation of protein molecules.
Uremia is a biochemical abnormality that includes S/ Sx.
In the fasting state, the carbon skeletons of the amino acids produce glucose, ketone bodies, and CO2 + H2O.
The carbon skeletons of the amino acids produce six major products: Pyruvate, Acetyl-CoA, α-ketoglutarate, Succinyl-CoA, Fumarate.
Hyperammonemia is a rise in ammonia level due to defects in urea cycle, which is a medical emergency due to neurotoxic effects on the CNS.
In the well-fed state, the liver can convert intermediates of amino acid metabolism to glycogen and triacylglycerols.
Protein is a fuel, with almost all amino acids generating NADH during degradation, which can enter the ETC for oxidative phosphorylation.
Metabolism of the carbon skeleton parallels metabolism of glucose and fatty acids.
Azotemia is a biochemical abnormality characterized by a high level of nitrogenous products in the blood, including BUN, creatinine, and urea.
Protein synthesis and protein degradation occur in the cell.
In the Ubiquitin-Proteasome Pathway, proteins attach covalently to ubiquitin, a small (76 AA), globular, non-enzymic protein.
The linkage of the α-carboxyl group of the C-terminalGly of ubiquitin to the ε-amino group of a Lys on the protein substrate is a three-step, enzyme-catalyzed, ATP-dependent process.
Glutamate, Glutamine, Proline, Arginine, Histidine are degraded to α-KG.
Glucogenic amino acids degradation leads to pyruvate, while ketogenic amino acids degradation leads to acetyl CoA.
Serine, Glycine, Cysteine, Alanine, Tryptophan, Threonine are degraded to pyruvate.
Glucogenic amino acids include Serine, Glycine, Cysteine, Alanine, Tryptophan, Threonine.
Methionine, Valine, Isoleucine, Threonine are degraded to succinyl CoA.
Ketogenic amino acids include Acetyl CoA, Tryptophan, Isoleucine, Threonine, Lysine.
Glucogenic amino acids yield pyruvate or TCA intermediates such as α-KG, succinyl CoA, fumarate, OAA.
Ketogenic amino acids yield ketone bodies or their precursors such as acetyl CoA or acetoacetyl CoA.
Leucine, Lysine, Tryptophan, Isoleucine, Threonine are degraded to acetyl CoA.
Polyubiquitinated proteins are recognized by proteasomes, a protease complex.
The proteasome unfolds, deubiquitinates, and cuts the target protein into fragments that are then further degraded to amino acids, which enter the amino acid pool.
Amino acid pool is in a steady state - the input to the amino acid pool is balanced by the output.
The amount of nitrogen ingested each day, mainly in the form of dietary protein, is equal to the amount of nitrogen excreted.
Cytosolic and mitochondrial fumarase and malate dehydrogenase communicate in the urea cycle.