Evidence for a novel racemization process of an asparaginyl residue in mouse lysozyme under physiological conditions

Keisuke Ueno, T. Ueda*, K. Sakai, Y. Abe, N. Hamasaki, M. Okamoto, T. Imoto

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


We examined chemical reactions in mouse lysozyme after incubation under physiological conditions (pH 7 and 37°C). After incubation for 8 weeks, racemization was observed specifically at Asn127 among the 19 Asp/Asn residues in mouse lysozyme. Furthermore, analysis of the primary structure showed that the racemized residue was not Asp, but Asn, which demonstrates that deamidation and isomerization did not occur. These results mean that this racemization occurs without forming a succinimide intermediate. This is the first example of D-asparaginyl formation in a protein occurring during the racemization process under physiological conditions.

Original languageEnglish (US)
Pages (from-to)199-205
Number of pages7
JournalCellular and Molecular Life Sciences
Issue number2
StatePublished - Jan 1 2005


  • Deterioration
  • Mouse lysozyme
  • Protein aging
  • Racemization

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Cell Biology

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