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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.
Leucine, like valine, regulates the first step of its pathway by inhibiting the action of the α-Isopropylmalate synthase. [18] Because leucine is synthesized by a diversion from the valine synthetic pathway, the feedback inhibition of valine on its pathway also can inhibit the synthesis of leucine.
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). This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-valine:tRNAVal ligase (AMP ...
Through manipulation of rodent diets, Rose was able to show that ten amino acids are essential for rats: lysine, tryptophan, histidine, phenylalanine, leucine, isoleucine, methionine, valine, and arginine, in addition to threonine. Rose's later work showed that eight amino acids are essential for adult human beings, with histidine also being ...
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 ...
Large aromatic residues (tyrosine, phenylalanine, tryptophan) and β-branched amino acids (threonine, valine, isoleucine) are favored to be found in β-strands in the middle of β-sheets. Different types of residues (such as proline ) are likely to be found in the edge strands in β-sheets, presumably to avoid the "edge-to-edge" association ...
At the very inception of the original, highly restricted definition (EFFDAxE), it was already evident that other amino acids could substitute at certain positions in the FFAT motifs of other homologs of OSBP, CERT and PITPNM1, in particular Y (tyrosine) in place of F at positions 2 and more so 3, also H (histidine) at position 3, and C (cysteine) or V (valine) at position 5. [1]
In enzymology, a valine-pyruvate transaminase (EC 2.6.1.66) is an enzyme that catalyzes the chemical reaction. L-valine + pyruvate 3-methyl-2-oxobutanoate + L-alanine. Thus, the two substrates of this enzyme are L-valine and pyruvate, whereas its two products are 3-methyl-2-oxobutanoate and L-alanine.