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  2. Sirtuin 4 - Wikipedia

    en.wikipedia.org/wiki/Sirtuin_4

    SIRT4 is a mitochondrial ADP-ribosyltransferase that inhibits mitochondrial glutamate dehydrogenase 1 activity, thereby downregulating insulin secretion in response to amino acids. [7] A deacetylation of malonyl-CoA decarboxylase enzyme by SIRT4 represses the enzyme activity, inhibiting fatty acid oxidation in muscle and liver cells.

  3. Glutamate dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Glutamate_dehydrogenase

    Beta cells secrete insulin in response to an increase in the ATP:ADP ratio, and, as amino acids are broken down by GLDH into α-ketoglutarate, this ratio rises and more insulin is secreted. SIRT4 is necessary to regulate the metabolism of amino acids as a method of controlling insulin secretion and regulating blood glucose levels.

  4. Kynurenine - Wikipedia

    en.wikipedia.org/wiki/Kynurenine

    l-Kynurenine is a metabolite of the amino acid l-tryptophan used in the production of niacin. Kynurenine is synthesized by the enzyme tryptophan dioxygenase , which is made primarily but not exclusively in the liver, and indoleamine 2,3-dioxygenase , which is made in many tissues in response to immune activation. [ 1 ]

  5. Kynurenic acid - Wikipedia

    en.wikipedia.org/wiki/Kynurenic_acid

    Kynurenic acid (KYNA or KYN) is a product of the normal metabolism of amino acid L-tryptophan. It has been shown that kynurenic acid possesses neuroactive activity. It acts as an antiexcitotoxic and anticonvulsant, most likely through acting as an antagonist at excitatory amino acid receptors. Because of this activity, it may influence ...

  6. Serine - Wikipedia

    en.wikipedia.org/wiki/Serine

    Serine (symbol Ser or S) [3] [4] is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated − NH +3 form under biological conditions), a carboxyl group (which is in the deprotonated − COO −

  7. Selenocysteine - Wikipedia

    en.wikipedia.org/wiki/Selenocysteine

    Like other natural proteinogenic amino acids, cysteine and selenocysteine have L chirality in the older D / L notation based on homology to D - and L-glyceraldehyde. In the newer R / S system of designating chirality, based on the atomic numbers of atoms near the asymmetric carbon, they have R chirality, because of the presence of sulfur or ...

  8. 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.

  9. Apamin - Wikipedia

    en.wikipedia.org/wiki/Apamin

    Apamin is an 18 amino acid globular peptide neurotoxin found in apitoxin (bee venom). [2] Dry bee venom consists of 2–3% of apamin. [3] Apamin selectively blocks SK channels, a type of Ca 2+-activated K + channel expressed in the central nervous system.