Regulation of Thioredoxin Peroxidase Activity by C-terminal Truncation

Koo, Kyung Hee; Lee, Songmi; Jeong, Seri; Kim, Eui‐Tae; Kim, Hyung Jung; Kim, Kanghwa; Song, Kiwon; Chae, Ho Zoon

doi:10.1006/abbi.2001.2700

Cited by 101 publications

(73 citation statements)

References 20 publications

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“…As exemplified by the tyrosine phosphorylation-dependent inactivation of Prx I, the peroxidase function of Prx can be regulated via various post-translational modifications. Such modifications also include threonine and serine phosphorylation (82,83), lysine acetylation (84), cysteine glutathionylation (85,86), cysteine nitrosylation (87), and limited proteolysis (88), although the biological relevance of these reactions remains unclear at the present time. Prxs also interact with numerous proteins, which might direct their cellular localization and sensitivity to oxidation (5).…”

Section: Discussionmentioning

confidence: 99%

Peroxiredoxin Functions as a Peroxidase and a Regulator and Sensor of Local Peroxides

Rhee

Woo

Kil

et al. 2012

Journal of Biological Chemistry

488

430

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Section: Discussionmentioning

confidence: 99%

Peroxiredoxin Functions as a Peroxidase and a Regulator and Sensor of Local Peroxides

Rhee

Woo

Kil

et al. 2012

Journal of Biological Chemistry

488

430

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“…The truncated enzyme was significantly more resilient against inactivation by hydrogen peroxide than the intact form [230]. Peroxidase assay of a series of recombinant C-terminal truncation mutants (Δ192, Δ191, Δ188, Δ184, Δ176, and Δ165) revealed that thioredoxin peroxidase could be inactivated (Δ192), reactivated (Δ191-Δ176) and reinactivated (Δ165) by serial truncation from C-terminus.…”

Section: Site Directed Mutagenesismentioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

COC

137

107

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Hydrogen peroxide is a substrate or side-product in many enzyme-catalyzed reactions. For example, it is a side-product of oxidases, resulting from the re-oxidation of FAD with molecular oxygen, and it is a substrate for peroxidases and other enzymes. However, hydrogen peroxide is able to chemically modify the peptide core of the enzymes it interacts with, and also to produce the oxidation of some cofactors and prostetic groups (e.g., the hemo group). Thus, the development of strategies that may permit to increase the stability of enzymes in the presence of this deleterious reagent is an interesting target. This enhancement in enzyme stability has been attempted following almost all available strategies: site-directed mutagenesis (eliminating the most reactive moieties), medium engineering (using stabilizers), immobilization and chemical modification (trying to generate hydrophobic environments surrounding the enzyme, to confer higher rigidity to the protein or to generate oxidation-resistant groups), or the use of systems capable of decomposing hydrogen peroxide under very mild conditions. If hydrogen peroxide is just a side-product, its immediate removal has been reported to be the best solution. In some cases, when hydrogen peroxide is the substrate and its decomposition is not a sensible solution, researchers coupled one enzyme generating hydrogen peroxide "in situ" to the target enzyme resulting in a continuous supply of this reagent at low concentrations thus preventing enzyme inactivation.This review will focus on the general role of hydrogen peroxide in biocatalysis, the main mechanisms of enzyme inactivation produced by this reactive and the different strategies used to prevent enzyme inactivation caused by this "dangerous liaison". Outlook

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“…The intact positive charge of Lys 191 in the C terminus of yeast Prx is important for the reducing activity and resistance of the protein to superoxidation by H 2 O 2 (15,30,31). We next tested whether the lysine residues in human Prx (Lys 197 in Prx I; Lys 196 in Prx II), corresponding to Lys 191 of yeast Prx, were acetylation sites.…”

Section: Identification Of 22-kda Proteins: Prx I and Prx Iimentioning

confidence: 99%

“…ROS are generated in cells in response to several types of environmental stress that lead to apoptosis and cell death (37). Prx I and Prx II play a role in modulating cellular response to ROS (30,31). LAPC4 cells, in which there is an accumulation of acetylated Prx I, H 2 O 2 concentrations (0.5 mM) that induce 100% of LNCaP and HFS cells to undergo apoptosis and cell death (Fig.…”

Section: Sensitivity To H2o2-induced Cell Death Of Lapc4 Lncap and mentioning

confidence: 99%

HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation

Parmigiani

Venta-Perez

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

284

234

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Eighteen histone deacetylases (HDACs) are present in humans, categorized into two groups: zinc-dependent enzymes (HDAC1-11) and NAD ؉ -dependent enzymes (sirtuins 1-7). Among zinc-dependent HDACs, HDAC6 is unique. It has a cytoplasmic localization, two catalytic sites, a ubiquitin-binding site, and it selectively deacetylases ␣-tubulin and Hsp90. Here, we report the discovery that the redox regulatory proteins, peroxiredoxin (Prx) I and Prx II are specific targets of HDAC6. Prx are antioxidants enzymes whose main function is H2O2 reduction. Prx are elevated in many cancers and neurodegenerative diseases. The acetylated form of Prx accumulates in the absence of an active HDAC6. Acetylation of Prx increases its reducing activity, its resistance to superoxidation, and its resistance to transition to highmolecular-mass complexes. Thus, HDAC6 and Prx are targets for modulating intracellular redox status in therapeutic strategies for disorders as disparate as cancers and neurodegenerative diseases.acetylation ͉ hydrogen peroxide ͉ histone deacetylase inhibitors

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Regulation of Thioredoxin Peroxidase Activity by C-terminal Truncation

Cited by 101 publications

References 20 publications

Peroxiredoxin Functions as a Peroxidase and a Regulator and Sensor of Local Peroxides

Peroxiredoxin Functions as a Peroxidase and a Regulator and Sensor of Local Peroxides

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation

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