In:
The FEBS Journal, Wiley, Vol. 285, No. 7 ( 2018-04), p. 1277-1289
Abstract:
Nonenzymatic acetylation of Lys side chains (Lys‐ SC s) by various in vivo reactive molecules has been suggested to play novel regulatory roles. Ubiquitin ( UB ) has seven Lys residues that are utilized for synthesis of specific poly‐ UB chains. To understand the nature of these Lys‐ SC modifications, the chemical acetylation rate and p K a and Hill coefficient of each UB ‐Lys‐ SC were measured. Mutagenesis studies combined with the determination of activation energy indicated that specific neighboring residues of the Lys‐ SC s have a potential catalytic activity during nonenzymatic acetylation. Based on the shared chemistry between nonenzymatic Lys acetylation and ubiquitylation, the characterized chemical properties of the UB ‐Lys‐ SC s could be a reference for deciphering both mechanisms. Our NMR approaches could be useful for studying general nonenzymatic Lys acylations of various proteins.
Type of Medium:
Online Resource
ISSN:
1742-464X
,
1742-4658
DOI:
10.1111/febs.2018.285.issue-7
Language:
English
Publisher:
Wiley
Publication Date:
2018
detail.hit.zdb_id:
2172518-4
SSG:
12
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