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2 reference results for: Valine

Columbia Encyclopedia

valine, organic compound, one of the 22 α-amino acids commonly found in animal proteins. Only the l-stereoisomer appears in mammalian protein. It is one of several essential amino acids needed in the diet, as the human body cannot synthesize it from simpler metabolites. Young adults need about 23 mg of this amino acid per day per kilogram (10 mg per lb) of body weight. Valine can be degraded into simpler compounds by the enzymes of the body; an inherited defect in one of the enzymes involved in this process results in a rare disorder called maple syrup urine disease. Valine contributes to the structure of proteins into which it has been incorporated by the tendency of its side chain to participate in hydrophobic interactions. The structure of valine was established in 1906, after it had been first isolated from albumin in 1879. See isoleucine.

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Wikipedia

Valine (abbreviated as Val or V) is an α-amino acid with the chemical formula HO₂CCH(NH₂)CH(CH₃)₂. L-Valine is one of 20 proteogenic amino acids. Its codons are GUU, GUC, GUA, and GUG. This essential amino acid is classified as nonpolar. Along with leucine and isoleucine, valine is a branched-chain amino acid. It is named after the plant valerian. In sickle-cell disease, valine substitutes for the hydrophilic amino acid glutamic acid in hemoglobin. Because valine is hydrophobic, the hemoglobin does not fold correctly.

Biosynthesis

Valine is an essential amino acid, hence it must be ingested, usually as a component of proteins. It is synthesized in plants via several steps starting from pyruvic acid. The initial part of the pathway also leads to leucine. The intermediate α-ketovalerate undergoes reductive amination with glutamate. Enzymes involved in this biosynthesis include: