Deamidation is a chemical reaction in which an amide functional group in the side chain of the amino acids asparagine or glutamine is removed or converted to another functional group.

In proteins and peptides, deamidation usually happens on asparagine (Asn) or glutamine (Gln) residues as a post-translational modification (PTM) to produce aspartic acid (Asp) or glutamic acid (Glu) [1,2]. …

Jul 23, 2025 · Deamidation is a naturally occurring chemical modification that affects proteins after they have been created within living organisms. This spontaneous process involves a change to specific …

Jun 5, 2025 · Protein deamidation is a spontaneous, irreversible post-translational modification (PTM) that has gained considerable attention for its role in cellular aging, disease progression, and the …

Deamidation is a nonenzymatic post-translational modification of asparagine to aspartic acid or glutamine to glutamic acid, converting an uncharged amino acid to a negatively charged residue.

May 5, 2024 · Deamination is the removal of an amine group from a molecule, crucial in amino acid catabolism, while deamidation involves removing an amide group, impacting protein stability.

Deamidation of proteins, which is usually slowed by 3D structure, occurs primarily at Asn except in very long-lived proteins where Gln deamidation is also observed.

The meaning of DEAMIDATE is to remove the amido group from (a compound).

Apr 22, 2020 · Here, we report that the enzyme carbamoyl-phosphate synthetase, aspartyl transcarbamoylase, and dihydroorotase (CAD) deamidates the RelA subunit of NF-κB in cancer cells …

Deamidation is a chemical process that involves the removal of an amide functional group from an amino acid. This reaction can be triggered by various factors such as high pH, temperature, and ionic …