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Lysine ball and stick model spinning. Lysine (symbol Lys or K) [2] is an α-amino acid that is a precursor to many proteins.Lysine contains an α-amino group (which is in the protonated −NH + 3 form when the lysine is dissolved in water at physiological pH), an α-carboxylic acid group (which is in the deprotonated −COO − form when the lysine is dissolved in water at physiological pH ...
The free fatty acids and glycerol are then released into the blood. A diagrammatic illustration of the transport of free fatty acids in the blood attached to plasma albumin, its diffusion across the cell membrane using a protein transporter, and its activation, using ATP, to form acyl-CoA in the cytosol. The illustration is of a 12 carbon fatty ...
It is produced during the breakdown of glucose, fatty acids, and amino acids, and is used in the synthesis of many other biomolecules, including cholesterol, fatty acids, and ketone bodies. Acetyl-CoA is also a key molecule in the citric acid cycle , which is a series of chemical reactions that occur in the mitochondria of cells and is ...
Alanine (symbol Ala or A), [4] or α-alanine, is an α-amino acid that is used in the biosynthesis of proteins. It contains an amine group and a carboxylic acid group, both attached to the central carbon atom which also carries a methyl group side chain. Consequently it is classified as a nonpolar, aliphatic α-amino acid.
In the kidneys, the enzyme AGAT catalyzes the conversion of two amino acids — arginine and glycine — into guanidinoacetate (also called glycocyamine or GAA), which is then transported in the blood to the liver. A methyl group is added to GAA from the amino acid methionine by the enzyme GAMT, forming non-phosphorylated creatine. This is then ...
Threonine (symbol Thr or T) [2] is an amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH + 3 form when dissolved in water), a carboxyl group (which is in the deprotonated −COO − form when dissolved in water), and a side chain containing a hydroxyl group , making it a ...
Coupling of two amino acids in solution. The unprotected amine of one reacts with the unprotected carboxylic acid group of the other to form a peptide bond.In this example, the second reactive group (amine/acid) in each of the starting materials bears a protecting group.
Hydroxyproline is produced by hydroxylation of the amino acid proline by the enzyme prolyl hydroxylase following protein synthesis (as a post-translational modification). The enzyme catalyzed reaction takes place in the lumen of the endoplasmic reticulum .