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

K. Ueno, Tadashi Ueda, K. Sakai, Yoshito Abe, N. Hamasaki, M. Okamoto, T. Imoto

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

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
Pages (from-to)199-205
Number of pages7
JournalCellular and Molecular Life Sciences
Volume62
Issue number2
DOIs
Publication statusPublished - Jan 1 2005

Fingerprint

Muramidase
Viperidae
Physiological Phenomena
Proteins
succinimide

All Science Journal Classification (ASJC) codes

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

Cite this

Evidence for a novel racemization process of an asparaginyl residue in mouse lysozyme under physiological conditions. / Ueno, K.; Ueda, Tadashi; Sakai, K.; Abe, Yoshito; Hamasaki, N.; Okamoto, M.; Imoto, T.

In: Cellular and Molecular Life Sciences, Vol. 62, No. 2, 01.01.2005, p. 199-205.

Research output: Contribution to journalArticle

@article{622d768aba0643229b4008767b633db0,
title = "Evidence for a novel racemization process of an asparaginyl residue in mouse lysozyme under physiological conditions",
abstract = "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.",
author = "K. Ueno and Tadashi Ueda and K. Sakai and Yoshito Abe and N. Hamasaki and M. Okamoto and T. Imoto",
year = "2005",
month = "1",
day = "1",
doi = "10.1007/s00018-004-4412-5",
language = "English",
volume = "62",
pages = "199--205",
journal = "Cellular and Molecular Life Sciences",
issn = "1420-682X",
publisher = "Birkhauser Verlag Basel",
number = "2",

}

TY - JOUR

T1 - Evidence for a novel racemization process of an asparaginyl residue in mouse lysozyme under physiological conditions

AU - Ueno, K.

AU - Ueda, Tadashi

AU - Sakai, K.

AU - Abe, Yoshito

AU - Hamasaki, N.

AU - Okamoto, M.

AU - Imoto, T.

PY - 2005/1/1

Y1 - 2005/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=13244257063&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=13244257063&partnerID=8YFLogxK

U2 - 10.1007/s00018-004-4412-5

DO - 10.1007/s00018-004-4412-5

M3 - Article

VL - 62

SP - 199

EP - 205

JO - Cellular and Molecular Life Sciences

JF - Cellular and Molecular Life Sciences

SN - 1420-682X

IS - 2

ER -