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Valine (symbol Val or V) [4] is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH 3 + form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side chain isopropyl group, making it a non-polar aliphatic amino acid.
A tetrapeptide (example: Val-Gly-Ser-Ala) with green highlighted N-terminal α-amino acid (example: L-valine) and blue marked C-terminal α-amino acid (example: L-alanine). The C-terminus (also known as the carboxyl-terminus , carboxy-terminus , C-terminal tail , carboxy tail , C-terminal end , or COOH-terminus ) is the end of an amino acid ...
The N-terminus is the first part of the protein that exits the ribosome during protein biosynthesis.It often contains signal peptide sequences, "intracellular postal codes" that direct delivery of the protein to the proper organelle.
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), and a side chain (CH 2) 4 NH 2 (which ...
In enzymology, a valine—tRNA ligase (EC 6.1.1.9) is an enzyme that catalyzes the chemical reaction. ATP + L-valine + tRNAVal AMP + diphosphate + L-valyl-tRNAVal The 3 substrates of this enzyme are ATP, L-valine, and tRNA(Val), whereas its 3 products are AMP, diphosphate, and L-valyl-tRNA(Val).
Efforts to understand how proteins are encoded began after DNA's structure was discovered in 1953. The key discoverers, English biophysicist Francis Crick and American biologist James Watson, working together at the Cavendish Laboratory of the University of Cambridge, hypothesied that information flows from DNA and that there is a link between DNA and proteins. [2]
In enzymology, a valine dehydrogenase (NADP +) (EC 1.4.1.8) is an enzyme that catalyzes the chemical reaction. L-valine + H 2 O + NADP + 3-methyl-2-oxobutanoate + NH 3 + NADPH + H +. The 3 substrates of this enzyme are L-valine, H 2 O, and NADP +, whereas its 4 products are 3-methyl-2-oxobutanoate, NH 3, NADPH, and H +.
The compound is a structural analog of valeric acid and also an isomer of the more common amino acid valine. [2] Like most other α-amino acids , norvaline is chiral . It is a white, water-soluble solid.