Evidence for a novel racemization process of an asparaginyl residue in mouse lysozyme under physiological conditions.
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.
Ueno
K
K
Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka, 812-8581, Japan.
Ueda
T
T
Sakai
K
K
Abe
Y
Y
Hamasaki
N
N
Okamoto
M
M
Imoto
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001216:Asparagine / Q000737:chemistry*; D001224:Aspartic Acid / Q000032:analysis / Q000737:chemistry; D051379:Mice; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry; D013237:Stereoisomerism; D013997:Time Factors
D010455:Peptides; D001224:Aspartic Acid; D001216:Asparagine; D009113:Muramidase