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  2. Leucine - Wikipedia

    en.wikipedia.org/wiki/Leucine

    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 ...

  3. Essential amino acid - Wikipedia

    en.wikipedia.org/wiki/Essential_amino_acid

    The distinction between essential and non-essential amino acids is somewhat unclear, as some amino acids can be produced from others. The sulfur-containing amino acids, methionine and homocysteine, can be converted into each other but neither can be synthesized de novo in humans. Likewise, cysteine can be made from homocysteine but cannot be ...

  4. Branched-chain amino acid - Wikipedia

    en.wikipedia.org/wiki/Branched-chain_amino_acid

    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]

  5. 3-Methylcrotonyl-CoA carboxylase deficiency - Wikipedia

    en.wikipedia.org/wiki/3-Methylcrotonyl-CoA...

    This enzyme plays an essential role in breaking down proteins from the diet. Specifically, the enzyme is responsible for the fourth step in processing leucine. If a mutation in the MCCC1 or MCCC2 gene reduces or eliminates the activity of 3-methylcrotonyl-CoA carboxylase, the body is unable to process leucine properly.

  6. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Both are produced as zymogens, meaning they are initially found in their inactive state and after cleavage though a hydrolysis reaction, they becomes activated. [2] Non-covalent interactions such as hydrogen bonding between the peptide backbone and the catalytic triad help increase reaction rates, allowing these peptidases to cleave many ...

  7. Transamination - Wikipedia

    en.wikipedia.org/wiki/Transamination

    Transamination is mediated by several types of aminotransferase enzymes. An aminotransferase may be specific for an individual amino acid, or it may be able to process any member of a group of similar ones, for example the branched-chain amino acids, which comprises valine, isoleucine, and leucine.

  8. Trace element - Wikipedia

    en.wikipedia.org/wiki/Trace_element

    A trace element is a chemical element of a minute quantity, a trace amount, especially used in referring to a micronutrient, [1] [2] but is also used to refer to minor elements in the composition of a rock, or other chemical substance. In nutrition, trace elements are classified into two groups: essential trace elements, and non-essential trace ...

  9. α-Ketoisocaproic acid - Wikipedia

    en.wikipedia.org/wiki/Α-Ketoisocaproic_acid

    Leucine is an essential amino acid, and its degradation is critical for many biological duties. [ 3 ] α-KIC is produced in one of the first steps of the pathway by branched-chain amino acid aminotransferase by transferring the amine on L-leucine onto alpha ketoglutarate , and replacing that amine with a ketone .