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  2. Asparagine - Wikipedia

    en.wikipedia.org/wiki/Asparagine

    Asparagine (symbol Asn or N [2]) 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), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side chain carboxamide, classifying it as a polar (at physiological pH), aliphatic ...

  3. Essential amino acid - Wikipedia

    en.wikipedia.org/wiki/Essential_amino_acid

    These six are alanine, aspartic acid, asparagine, glutamic acid, serine, [2] and selenocysteine (considered the 21st amino acid). Pyrrolysine (considered the 22nd amino acid), [3] which is proteinogenic only in certain microorganisms, is not used by and therefore non-essential for most organisms, including humans.

  4. Asparaginase - Wikipedia

    en.wikipedia.org/wiki/Asparaginase

    Asparaginase is an enzyme that is used as a medication and in food manufacturing. [6] [7] As a medication, L-asparaginase is used to treat acute lymphoblastic leukemia (ALL) and lymphoblastic lymphoma (LBL). [6] It is given by injection into a vein, or muscle. [6] A pegylated version is also available. [8] In food manufacturing it is used to ...

  5. 3-Hydroxyasparagine - Wikipedia

    en.wikipedia.org/wiki/3-hydroxyasparagine

    3-Hydroxyasparagine also known as β-hydroxyasparagine (beta-hydroxyasparagine) is a modified asparagine amino acid. It appears in posttranslational modification of cbEGF-like domains which can occur in humans and other Eukaryotes. The amino acid code used for this is Hyn. The modified amino acid residue is found in fibrillin-1. [1]

  6. Asparagine synthetase - Wikipedia

    en.wikipedia.org/wiki/Asparagine_synthetase

    Escherichia coli derived asparagine synthetase is a dimeric protein with each subunit folding into two distinct domains. [4] The N-terminal region consists of two layers of six-stranded antiparallel β-sheets between which is the active site responsible for the hydrolysis of glutamine. [4]

  7. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    In the asparagine synthetase reaction, ATP is used to activate aspartate, forming β-aspartyl-AMP. Glutamine donates an ammonium group, which reacts with β-aspartyl-AMP to form asparagine and free AMP. The biosynthesis of aspartate and asparagine from oxaloacetate. Two asparagine synthetases are found in bacteria.

  8. Asparagine—tRNA ligase - Wikipedia

    en.wikipedia.org/wiki/Asparagine—tRNA_ligase

    The systematic name of this enzyme class is L-asparagine:tRNAAsn ligase (AMP-forming). Other names in common use include asparaginyl-tRNA synthetase , asparaginyl-transfer ribonucleate synthetase , asparaginyl transfer RNA synthetase , asparaginyl transfer ribonucleic acid synthetase , asparagyl-transfer RNA synthetase , and asparagine translase .

  9. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    Met is essential for humans. Always the first amino acid to be incorporated into a protein, it is sometimes removed after translation. Like cysteine, it contains sulfur, but with a methyl group instead of hydrogen. This methyl group can be activated, and is used in many reactions where a new carbon atom is being added to another molecule ...