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  2. N-Acetyl-L-tyrosine - Wikipedia

    en.wikipedia.org/wiki/N-Acetyl-L-tyrosine

    N-Acetyl-L-tyrosine is an amino acid, an N-acetyl derivative of tyrosine. It is used for parenteral nutrition and as a dietary supplement. [1] [2] [3] See also.

  3. Nitrotyrosine - Wikipedia

    en.wikipedia.org/wiki/Nitrotyrosine

    Research shows that nitrotyrosine levels can be reduced by N-acetyl cysteine, [10] [11] which is a precursor to glutathione, one of the body's primary endogenous antioxidants. Nitrotyrosine levels have been linked to cerebral ischemia and edema, for which NAC has also been proven as a potential treatment. [12]

  4. Tyrosine - Wikipedia

    en.wikipedia.org/wiki/Tyrosine

    In addition to the common amino acid L-tyrosine, which is the para isomer (para-tyr, p-tyr or 4-hydroxyphenylalanine), there are two additional regioisomers, namely meta-tyrosine (also known as 3-hydroxyphenylalanine, L-m-tyrosine, and m-tyr) and ortho-tyrosine (o-tyr or 2-hydroxyphenylalanine), that occur in nature.

  5. N-acetylneuraminate 7-O (or 9-O)-acetyltransferase - Wikipedia

    en.wikipedia.org/wiki/N-acetylneuraminate_7-O(or...

    Schauer R (May 1970). "[Biosynthesis of N-acetyl-O-acetylneuraminic acids. I. Incorporation of (14C) acetate into sections of the submaxillary salivary gland of ox and horse]". Hoppe-Seyler's Zeitschrift für Physiologische Chemie. 351 (5): 595–602. PMID 5446640. Schauer R (June 1970). "[Biosynthesis of N-acetyl-O-acetylneuraminic acids. II.

  6. Chymotrypsin - Wikipedia

    en.wikipedia.org/wiki/Chymotrypsin

    The main substrates of chymotrypsin are peptide bonds in which the amino acid N-terminal to the bond is a tryptophan, tyrosine, phenylalanine, or leucine. Like many proteases, chymotrypsin also hydrolyses amide bonds in vitro, a virtue that enabled the use of substrate analogs such as N-acetyl-L-phenylalanine p-nitrophenyl amide for enzyme assays.

  7. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    [2] The conversion of glutamate to glutamine is regulated by glutamine synthetase (GS) and is a key step in nitrogen metabolism. [2] This enzyme is regulated by at least four different mechanisms: 1. Repression and depression due to nitrogen levels; 2. Activation and inactivation due to enzymatic forms (taut and relaxed); 3.

  8. Phenylalanine N-acetyltransferase - Wikipedia

    en.wikipedia.org/wiki/Phenylalanine_N-acetyl...

    In enzymology, a phenylalanine N-acetyltransferase (EC 2.3.1.53) is an enzyme that catalyzes the chemical reaction. acetyl-CoA + L-phenylalanine CoA + N-acetyl-L-phenylalanine. Thus, the two substrates of this enzyme are acetyl-CoA and L-phenylalanine, whereas its two products are CoA and N-acetyl-L-phenylalanine.

  9. Talk:N-Acetyl-L-tyrosine - Wikipedia

    en.wikipedia.org/wiki/Talk:N-Acetyl-L-tyrosine

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