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  2. Aminoacyl tRNA synthetase - Wikipedia

    en.wikipedia.org/wiki/Aminoacyl_tRNA_synthetase

    The synthetase first binds ATP and the corresponding amino acid (or its precursor) to form an aminoacyl-adenylate, releasing inorganic pyrophosphate (PPi).The adenylate-aaRS complex then binds the appropriate tRNA molecule's D arm, and the amino acid is transferred from the aa-AMP to either the 2'- or the 3'-OH of the last tRNA nucleotide (A76) at the 3'-end.

  3. Aminoacyl-tRNA - Wikipedia

    en.wikipedia.org/wiki/Aminoacyl-tRNA

    An aminoacyl-tRNA, with the tRNA above the arrow and a generic amino acid below the arrow. Most of the tRNA structure is shown as a simplified, colorful ball-and-stick model; the terminal adenosine and the amino acid are shown as structural formulas. The arrow indicates the ester linkage between the amino acid and tRNA.

  4. Wobble base pair - Wikipedia

    en.wikipedia.org/wiki/Wobble_base_pair

    The alpha helix was the recognizable structure for the aminoacyl tRNA synthetase and thus the synthetase does not connect the amino acid alanine with the tRNA for alanine. This wobble base pairing is essential for the use of the amino acid alanine in E. coli and its significance here would imply significance in many related species. [ 10 ]

  5. Amino acid activation - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_activation

    Amino acid activation (also known as aminoacylation or tRNA charging) refers to the attachment of an amino acid to its respective transfer RNA (tRNA). The reaction occurs in the cell cytosol and consists of two steps: first, the enzyme aminoacyl tRNA synthetase catalyzes the binding of adenosine triphosphate (ATP) to a corresponding amino acid, forming a reactive aminoacyl adenylate ...

  6. KARS (gene) - Wikipedia

    en.wikipedia.org/wiki/KARS_(gene)

    Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. Lysyl-tRNA synthetase is a homodimer localized to the cytoplasm which belongs to the class II family of tRNA synthetases. It has been shown to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis [7]

  7. Aminoacyltransferase - Wikipedia

    en.wikipedia.org/wiki/Aminoacyltransferase

    The general structure of an amine. Aminoacyltransferases (EC 2.3.2) are acyltransferase enzymes which act upon an amino group. For instance, aminoacyl tRNA synthetases attach an aminoacid through esterification to the corresponding tRNA. The activation of amino acids it aminoacyl-tRNA synthetase requires hydrolysis of ATP to AMP plus PP i.

  8. Aminoacyl tRNA synthetases, class II - Wikipedia

    en.wikipedia.org/wiki/Aminoacyl_tRNA_synthetases...

    Aminoacyl-tRNA synthetases, class II is a family of proteins. These proteins catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have a limited sequence homology .

  9. EPRS - Wikipedia

    en.wikipedia.org/wiki/EPRS

    The protein encoded by this gene is a multifunctional aminoacyl-tRNA synthetase that catalyzes the aminoacylation of glutamic acid and proline tRNA species. [ 6 ] Phosphorylation of EPRS is reported to be essential for the formation of GAIT (Gamma-interferon Activated Inhibitor of Translation) complex that regulates the translation of multiple ...