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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. 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 .

  4. PNGase F - Wikipedia

    en.wikipedia.org/wiki/PNGase_F

    Peptide:N-glycosidase F, commonly referred to as PNGase F, is an amidase of the peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase class. PNGase F works by cleaving between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and complex oligosaccharides from N-linked glycoproteins and glycopeptides.

  5. Deamidation - Wikipedia

    en.wikipedia.org/wiki/Deamidation

    Typically, asparagine is converted to aspartic acid or isoaspartic acid. Glutamine is converted to glutamic acid or pyroglutamic acid (5-oxoproline). In a protein or peptide, these reactions are important because they may alter its structure, stability or function and may lead to protein degradation. The net chemical change is the addition of a ...

  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. N-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/N-linked_glycosylation

    The different types of lipid-linked oligosaccharide (LLO) precursor produced in different organisms.. N-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom (the amide nitrogen of an asparagine (Asn) residue of a protein), in a process called N-glycosylation, studied in ...

  8. Asparagine peptide lyase - Wikipedia

    en.wikipedia.org/wiki/Asparagine_peptide_lyase

    Asparagine peptide lyase are one of the seven groups in which proteases, also termed proteolytic enzymes, peptidases, or proteinases, are classified according to their catalytic residue. The catalytic mechanism of the asparagine peptide lyases involves an asparagine residue acting as nucleophile to perform a nucleophilic elimination reaction ...

  9. Asparagine synthase (glutamine-hydrolysing) - Wikipedia

    en.wikipedia.org/wiki/Asparagine_synthase...

    Asparagine synthase (glutamine-hydrolysing) (EC 6.3.5.4, asparagine synthetase (glutamine-hydrolysing), glutamine-dependent asparagine synthetase, asparagine synthetase B, AS, AS-B) is an enzyme with systematic name L-aspartate:L-glutamine amido-ligase (AMP-forming).