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  2. Arginine - Wikipedia

    en.wikipedia.org/wiki/Arginine

    Only the l-arginine (symbol Arg or R) enantiomer is found naturally. [1] Arg residues are common components of proteins. It is encoded by the codons CGU, CGC, CGA, CGG, AGA, and AGG. [2] The guanidine group in arginine is the precursor for the biosynthesis of nitric oxide. [3] Like all amino acids, it is a white, water-soluble solid.

  3. Arginase - Wikipedia

    en.wikipedia.org/wiki/Arginase

    The second isozyme, Arginase II, has been implicated in the regulation of intracellular arginine/ornithine levels. It is located in mitochondria of several tissues in the body, with most abundance in the kidney and prostate. It may be found at lower levels in macrophages, lactating mammary glands, and brain. [5]

  4. Arginylation - Wikipedia

    en.wikipedia.org/wiki/Arginylation

    In arginylation, arginine (pictured above) is added to proteins. Arginylation is a post-translational modification in which proteins are modified by the addition of arginine (Arg) at the N-terminal amino group or side chains of reactive amino acids by the enzyme, arginyltransferase (ATE1). Recent studies have also revealed that hundreds of ...

  5. Composition of the human body - Wikipedia

    en.wikipedia.org/wiki/Composition_of_the_human_body

    Parts-per-million cube of relative abundance by mass of elements in an average adult human body down to 1 ppm. About 99% of the mass of the human body is made up of six elements: oxygen, carbon, hydrogen, nitrogen, calcium, and phosphorus. Only about 0.85% is composed of another five elements: potassium, sulfur, sodium, chlorine, and magnesium ...

  6. Arginine and proline metabolism - Wikipedia

    en.wikipedia.org/wiki/Arginine_and_proline...

    Arginine and proline metabolism is one of the central pathways for the biosynthesis of the amino acids arginine and proline from glutamate. The pathways linking arginine, glutamate, and proline are bidirectional. Thus, the net utilization or production of these amino acids is highly dependent on cell type and developmental stage.

  7. Arginylglycylaspartic acid - Wikipedia

    en.wikipedia.org/wiki/Arginylglycylaspartic_acid

    Arginylglycylaspartic acid (RGD) is the most common peptide motif responsible for cell adhesion to the extracellular matrix (ECM), found in species ranging from Drosophila to humans.

  8. Nitric oxide synthase - Wikipedia

    en.wikipedia.org/wiki/Nitric_oxide_synthase

    Nitric oxide synthases produce NO by catalysing a five-electron oxidation of a guanidino nitrogen of L-arginine (L-Arg). Oxidation of L-Arg to L-citrulline occurs via two successive monooxygenation reactions producing N ω-hydroxy-L-arginine (NOHLA) as an intermediate. 2 mol of O 2 and 1.5 mol of NADPH are consumed per mole of NO formed. [3]

  9. Argininemia - Wikipedia

    en.wikipedia.org/wiki/Argininemia

    Argininemia is an autosomal recessive urea cycle disorder where a deficiency of the enzyme arginase causes a buildup of arginine and ammonia in the blood.Ammonia, which is formed when proteins are broken down in the body, is toxic if levels become too high; the nervous system is especially sensitive to the effects of excess ammonia.

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