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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 ...
In Corynebacterium glutamicum, BrnFE exports branched chain amino acids isoleucine, leucine, and valine, as well as methionine and homoserine. [3] [5] [8] The greatest induction of BrnFE expression occurs under high methionine concentrations, suggesting that methionine may actually be the native substrate rather than a branched-chain amino acid ...
Pages in category "Branched-chain amino acids" The following 8 pages are in this category, out of 8 total. This list may not reflect recent changes. ...
The BCAT enzyme catalyzes the conversion of BCAAs and α-ketoglutarate into branched chain α-keto acids and glutamate. The structure to the right of branched chain amino acid aminotransferase was found using X-ray diffraction with a resolution of 2.20 Å. The branched-chain amino acid aminotransferase found in this image was isolated from ...
Alloisoleucine is an amino acid with the formula CH 3 CH 2 CH(CH 3)CH(NH 2)CO 2 H. It exists as two enantiomers , of which the L derivative occurs naturally. L-Alloisoleucine occurs in healthy serum in only trace amounts, except for individuals suffering from maple syrup urine disease .
Two different clinical disorders have been attributed to a defect of branched-chain amino acid transamination: hypervalinemia and hyperleucine-isoleucinemia. [11] As there is also a gene encoding a mitochondrial form of this enzyme (BCAT2), mutations in either gene may contribute to these disorders.
The acetolactate synthase (ALS) enzyme (also known as acetohydroxy acid or acetohydroxyacid synthase, abbr. AHAS) [2] is a protein found in plants and micro-organisms. ALS catalyzes the first step in the synthesis of the branched-chain amino acids (valine, leucine, and isoleucine).
During branched-chain amino acid degradation, MCC performs a single step in the breakdown of leucine to eventually yield acetyl CoA and acetoacetate. [7] MCC catalyzes the carboxylation of 3-methylcrotonyl CoA to 3-methylglutaconyl CoA, a critical step for leucine and isovaleric acid catabolism in species including mammals, plants and bacteria.