ArticleScientific reports2016
Structural and activity characterization of human PHPT1 after oxidative modification.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
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- Molecular signatures written in bone proteins of 79 AD victims from Herculaneum and Pompeii.Scientific reports · 2022Article
- Indirect effect of alpha-1-antitrypsin on endotoxin-induced IL-1β secretion from human PBMCs.Frontiers in pharmacology · 2022Article
- Phospho-PTM proteomic discovery of novel EPO- modulated kinases and phosphatases, including PTPN18 as a positive regulator of EPOR/JAK2 Signaling.Cellular signalling · 2020Article
- Exercise and metformin counteract altered mitochondrial function in the insulin-resistant brain.JCI insight · 2019Article
- Insulin deficiency and intranasal insulin alter brain mitochondrial function: a potential factor for dementia in diabetes.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Natural Products Containing 'Rare' Organophosphorus Functional Groups.Molecules (Basel, Switzerland) · 2019Review
- The first in vivo multiparametric comparison of different radiation exposure biomarkers in human blood.PloS one · 2018Article
- Stimulation of Nipah Fusion: Small Intradomain Changes Trigger Extensive Interdomain Rearrangements.Biophysical journal · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Phosphohistidine phosphatase 1 (PHPT1), the only known phosphohistidine phosphatase in mammals, regulates phosphohistidine levels of several proteins including those involved in signaling, lipid metabolism, and potassium ion transport. While the high-resolution structure of human PHPT1 (hPHPT1) is available and residues important for substrate binding and catalytic activity have been reported, little is known about post-translational modifications that modulate hPHPT1 activity. Here we characterize the structural and functional impact of hPHPT1 oxidation upon exposure to a reactive oxygen species, hydrogen peroxide (H2O2). Specifically, liquid chromatography-tandem mass spectrometry was used to quantify site-specific oxidation of redox-sensitive residues of hPHPT1. Results from this study revealed that H2O2 exposure induces selective oxidation of hPHPT1 at Met95, a residue within the substrate binding region. Explicit solvent molecular dynamics simulations, however, predict only a minor effect of Met95 oxidation in the structure and dynamics of the apo-state of the hPHPT1 catalytic site, suggesting that if Met95 oxidation alters hPHPT1 activity, then it will do so by altering the stability of an intermediate state. Employing a novel mass spectrometry-based assay, we determined that H2O2-induced oxidation does not impact hPHPT1 function negatively; a result contrary to the common conception that protein oxidation is typically a loss-of-function modification.
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