Two Enzymes in One

Jang, Ho Hee; Lee, Kyun Oh; Hun, Yong; Jung, Bang Chul; Park, Soo Kwon; Park, Jin Ho; Lee, Jung Ro; Lee, Seung Sik; Moon, Jeong Chan; Yun, Jeong Won; Choi, Yeon Ok; Kim, Woe Yeon; Kang, Ji Seoun; Cheong, Gang-Won; Yun, Dae‐Jin; Rhee, Sue Goo; Cho, Moo Je; Lee, Sang Yeol

doi:10.1016/j.cell.2004.05.002

Cited by 681 publications

(380 citation statements)

References 36 publications

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“…The catalytic sites contain Cys-49 and Cys-169 in the conserved tripeptide Val-Cys-Pro (VCP) and form an intramolecular disulfide bond essential for the catalytic activity (21,27,28). When we compared these two AhpC proteins, their amino acid sequences were found to be almost identical, with only one point mutation, at residue 101, valine in the HD30 strain and methionine in the HC28 strain (data not shown).…”

Section: Resultsmentioning

confidence: 88%

“…Several functional studies of H. pylori AhpC have shown that the AhpCdeleted mutants have increased sensitivity to oxygen (15), overexpress neutrophil-activating protein (18), and accelerate inactivation of catalase (25). As a member of 2-Cys peroxiredoxins (17,21,31), AhpC has been shown to be Trx-dependent (17,27,32,33). The native structure of AhpC in S. typhimurium was shown to exist as a dimer (34,35).…”

Section: Discussionmentioning

confidence: 99%

“…The His 6 -fused AhpC was purified by using a native Ni-NTA column (Qiagen, Chatsworth, CA). The enzyme activity of the recombinant AhpC containing the added six His residues at the C terminus was measured according to previous reports (21,27). The purity of the purified recombinant AhpC was determined to be Ͼ99% based on SDS͞PAGE.…”

Section: Methodsmentioning

confidence: 99%

“…These results suggest that AhpC in H. pylori, in addition to providing its anti-oxidative activity, may also play an important role in the regulation of other cellular functions. It was indeed observed that yeast peroxiredoxins (Prxs) can switch from an enzymatic activity to a molecularchaperone function under oxidative stresses (27). However, there is no report on AhpC in prokaryotes regarding its structural modification or functional switch under oxidative stresses.…”

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confidence: 99%

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The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function

Chuang

Wu²,

Lo³

et al. 2006

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

132

105

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Helicobacter pylori, an oxygen-sensitive microaerophilic bacterium, contains many antioxidant proteins, among which alkylhydroperoxide reductase (AhpC) is the most abundant. The function of AhpC is to protect H. pylori from a hyperoxidative environment by reduction of toxic organic hydroperoxides. We have found that the sequence of AhpC from H. pylori is more homologous to mammalian peroxiredoxins than to eubacterial AhpC. We have also found that the protein structure of AhpC could shift from lowmolecular-weight oligomers with peroxide-reductase activity to high-molecular-weight complexes with molecular-chaperone function under oxidative stresses. Time-course study by following the quaternary structural change of AhpC in vivo revealed that this enzyme changes from low-molecular-weight oligomers under normal microaerobic conditions or short-term oxidative shock to high-molecular-weight complexes after severe long-term oxidative stress. This study revealed that AhpC of H. pylori acts as a peroxide reductase in reducing organic hydroperoxides and as a molecular chaperone for prevention of protein misfolding under oxidative stress.peroxiredoxin ͉ oxidative stress ͉ phylogenetic comparison ͉ dual functionality ͉ quaternary structural change

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Section: Resultsmentioning

confidence: 88%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function

Chuang

Wu²,

Lo³

et al. 2006

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

132

105

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show abstract

“…Upon peroxidatic Cys oxidation, 2‐Cys PRDX1 is structurally converted from a peroxidase enzyme to a molecular chaperone under stress conditions 9, 10. In addition to its peroxidase and chaperone functions, PRDX1 could also enhance natural killer cell cytotoxicity and suppress oncogenic proteins such as c‐Myc and c‐Abl 11, 12, 13.…”

Section: Introductionmentioning

confidence: 99%

Peroxiredoxin 1 – an antioxidant enzyme in cancer

Ding

Fan

2016

J Cellular Molecular Medi

171

131

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Peroxiredoxins (PRDXs), a ubiquitous family of redox‐regulating proteins, are reported of potential to eliminate various reactive oxygen species (ROS). As a major member of the antioxidant enzymes, PRDX1 can become easily over‐oxidized on its catalytically active cysteine induced by a variety of stimuli in vitro and in vivo. In nucleus, oligomeric PRDX1 directly associates with p53 or transcription factors such as c‐Myc, NF‐κB and AR, and thus affects their bioactivities upon gene regulation, which in turn induces or suppresses cell death. Additionally, PRDX1 in cytoplasm has anti‐apoptotic potential through direct or indirect interactions with several ROS‐dependent (redox regulation) effectors, including ASK1, p66Shc, GSTpi/JNK and c‐Abl kinase. PRDX1 is proven to be a versatile molecule regulating cell growth, differentiation and apoptosis. Recent studies have found that PRDX1 and/or PRDX1‐regulated ROS‐dependent signalling pathways play an important role in the progression and metastasis of human tumours, particularly in breast, oesophageal and lung cancers. In this paper, we review the structure, effector functions of PRDX1, its role in cancer and the pivotal role of ROS in anticancer treatment.

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Overview of Peroxiredoxins in Oxidant Defense and Redox Regulation

2011

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Peroxiredoxins are important hydroperoxide detoxification enzymes, yet have only come to the fore in recent years relative to the other major players in peroxide detoxification, heme-containing catalases and peroxidases, and glutathione peroxidases. These cysteine-dependent peroxidases exhibit high reactivity with hydrogen peroxide, organic hydroperoxides and peroxynitrite and play major roles not only in peroxide defense, but also in regulating peroxide-mediated cell signaling. This overview focuses on important peroxiredoxin features that have emerged over the past several decades with an emphasis on catalytic mechanism, regulation and biological function.

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Two Enzymes in One

Cited by 681 publications

References 36 publications

The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function

The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function

Peroxiredoxin 1 – an antioxidant enzyme in cancer

Overview of Peroxiredoxins in Oxidant Defense and Redox Regulation

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