The apparent deglycase activity of DJ-1 results from the conversion of free methylglyoxal present in fast equilibrium with hemithioacetals and hemiaminals-Reference-Cited by-同舟云学术

The apparent deglycase activity of DJ-1 results from the conversion of free methylglyoxal present in fast equilibrium with hemithioacetals and hemiaminals

Published:2019-12 Issue:49 Volume:294 Page:18863-18872
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Andreeva Anna,Bekkhozhin Zhanibek,Omertassova Nuriza,Baizhumanov Timur,Yeltay Gaziza,Akhmetali Mels,Toibazar Daulet,Utepbergenov Darkhan^ORCID

Funder

Nazarbayev University

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference25 articles.

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2. The Parkinson’s disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization;Canet-Avilés;Proc. Natl. Acad. Sci. U.S.A,2004

3. Hsp31 of Escherichia coli K-12 is glyoxalase III;Subedi;Mol. Microbiol,2011

4. Human DJ-1 and its homologs are novel glyoxalases;Lee;Hum. Mol. Genet,2012

5. Stereospecific mechanism of DJ-1 glyoxalases inferred from their hemithioacetal-containing crystal structures;Choi;FEBS J,2014

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