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Age-dependent deamidation of asparagine residues in proteins.

作者信息

Lindner H, Helliger W

机构信息

Institute of Medical Chemistry and Biochemistry, University of Innsbruck, Fritz-Preglstrasse 3, A-6020 Innsbruck, Austria.

出版信息

Exp Gerontol. 2001 Sep;36(9):1551-63. doi: 10.1016/s0531-5565(01)00140-1.

DOI:10.1016/s0531-5565(01)00140-1
PMID:11525877
Abstract

Nonenzymatic deamidation of peptides and proteins represents an important degradation reaction occurring in vitro in the course of isolation or storage and in vivo during development and/or aging of cells. This review first presents a synopsis of the influence of structure on deamidation reaction proceeding via a five-membered succinimide intermediate, followed by an outline of procedures for separation and detection of deamidated forms. Selected examples for in vitro and in vivo deamidation are reviewed including the possible biological consequences of this protein degradation. Finally, the reaction of protein methyltransferase with L-isoaspartyl- and D-aspartyl residues and its possible role in protein repair is elucidated.

摘要

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Age-dependent deamidation of asparagine residues in proteins.
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