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deamidation
A chemical reaction in which an amide functional group is removed from an organic compound.
In biochemistry, functions in the degradation of proteins via alteration of the amide-containing side chains of the amino acid residues Asn & Gln. Asn is converted to Asp or iso-Asp; Gln is converted to Glu.
Deamidation may be one of the factors that limit the useful lifetime of proteins.
Deamidation is more facile if the susceptible amino acid residue is adjacent to a small, flexible residue such as glycine. Deamidation reactions are more facile at elevated pH & temperature.
Deamidation may be enzymatically catalyzed by:
- protein N-terminal asparagine amidohydrolase (PNAA)
General
biochemistry
References
- Wikipedia: Deamidation
http://en.wikipedia.org/wiki/Deamidation
- Clarke S.
Propensity for spontaneous succinimide formation from aspartyl
and asparaginyl residues in cellular proteins
Int. J., Peptide Protein Res. 1987, 30:808-821
PMID: 3440704
- Stephenson RC and Clarke S.
Succinimide Formation from Aspartyl and Asparaginyl Peptides
as a Model for the Spontaneous Degradation of Proteins
J. Biol. Chem. 1989, 264:6164-6170
PMID: 2703484