Only a few side chains of the aminoacid residues usually found in proteins are suitable for the attachment of a mono- or oligo-saccharide (Table 2.1). A very common linkage involves the C(1) of N - acetylglucosamine and the amide group of asparagine. The structure (Fig. 2.1) is 2-acet...
Working on human asparagine synthetase, Coricello et al show that combining 3D variability analysis (3DVA) of cryo-EM data with MD simulations is a valid approach to study conformation of amino acid side chains that might regulate enzyme function. ...
While amino acids are necessary for life, not all of them can be produced naturally in the body. Of the20 amino acids, 11 can be produced naturally. Thesenonessential amino acidsare alanine, arginine, asparagine, aspartate, cysteine, glutamate, glutamine, glycine, proline, serine, and tyrosine...
Asparagine is an important nitrogen storage and transport molecule, but its accumulation as a free amino acid in crops has implications for food safety because free asparagine is a precursor for acrylamide formation during cooking and processing. Asparagine synthesis occurs by the amidation of aspartate...
Thus far, 15 unique mutations in the ASNS gene have been clinically associated with asparagine synthetase deficiency (ASD). Molecular modelling using the E. coli ASNS-B structure has revealed that most of the reported ASD substitutions are located near catalytic sites or within highly conserved ...
The Amino Acid Structure Chart and Reference Table Chart describes the biological properties and solubility of the 20 standard amino acids.
The crystal structure of isoaspartyl aminopeptidase/asparaginase (EcAIII), an enzyme belonging to the N-terminal nucleophile (Ntn)-hydrolases family, has been determined at 1.9- resolution for a complex obtained by cocrystallization with -aspartate, which is a product of both enzymatic reactions catal...
A complete structure of asparagine linked sugar chains of bovine IgG was determined to be as follows. This structure is inconsistent with the results obtained from myeloma proteins in that incomplete galactosylation occurred in the branch with α1→3 linked mannosyl residue.DOI...
The structure was determined at pH 5, where Asp24 is fully protonated. The relative orientation of the two extended helices in the A24D/D61N structure is different from that in the protonated form of the wild-type protein, also determined at pH 5. The C-terminal helix is rotated by ...
The former enzyme is an asparagines amidase that cleaves the N-glycosidic (amide) bond between the asparagines and the oligosaccharide chains. This cleavage gives rise to the free β-glycosylamine, and aspartic acid that remains in the protein in the original position of the asparagines. On ...