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

Authors
Type
Published Article
Journal
Cellular and molecular life sciences : CMLS
Publication Date
Volume
62
Issue
2
Pages
199–205
Identifiers
PMID: 15666091
Source
Medline

Abstract

We examined chemical reactions in mouse lysozyme after incubation under physiological conditions (pH 7 and 37 degrees 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.

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