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A branched-chain amino acid (BCAA) is an amino acid having an aliphatic side-chain with a branch (a central carbon atom bound to three or more carbon atoms). Among the proteinogenic amino acids, there are three BCAAs: leucine, isoleucine, and valine. [1] Non-proteinogenic BCAAs include 2-aminoisobutyric acid and alloisoleucine. Leucine ...
Plants, fungi, and bacteria are also distinguishable by their amino acid carbon isotopes. The compositions of the essential amino acids, which have more complex biosynthetic pathways, are particularly informative. Lysine, isoleucine, leucine, threonine, and valine all had significantly different δ 13 C values between at least two of these ...
The blood concentration of leucine and isoleucine is measured relative to other amino acids to determine if the newborn has a high level of branched-chain amino acids. Once the newborn is 2–3 days old the blood concentration of branched-chain amino acids like leucine is greater than 1000 μmol/L and alternative screening methods are used.
Leucine ball and stick model spinning. Leucine (symbol Leu or L) [3] is an essential amino acid that is used in the biosynthesis of proteins.Leucine is an α-amino acid, meaning 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 ...
Isoleucine is an essential component of many proteins. As an essential amino acid, isoleucine must be ingested or protein production in the cell will be disrupted. Fetal hemoglobin is one of the many proteins that require isoleucine. [12] Isoleucine is present in the gamma chain of fetal hemoglobin and must be present for the protein to form. [12]
Treatment consists of dietary protein restriction, particularly leucine. During acute episodes, glycine is sometimes given, which conjugates with isovalerate forming isovalerylglycine, or carnitine which has a similar effect. [citation needed] Elevated 3-hydroxyisovaleric acid is a clinical biomarker of biotin deficiency.
Mitochondrial branched-chain amino acid aminotransferases are the more ubiquitous of the two isoforms, present in all tissues in the mitochondria of the cell. [8] Pancreatic acinar tissue has been found to carry the highest levels of BCATm in the body [ 19 ] In addition, two homologs to normal BCATm have been found.
Mutations that cause the altered codon to produce an amino acid with similar functionality (e.g. a mutation producing leucine instead of isoleucine) are often classified as silent; if the properties of the amino acid are conserved, this mutation does not usually significantly affect protein function. [6]