ArticleUpsala journal of medical sciences2015
Phosphohistidine phosphatase 1 (PHPT1) also dephosphorylates phospholysine of chemically phosphorylated histone H1 and polylysine.
Article in Upsala journal of medical sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 23 citations in OpenAlex.
- Inhibition of PHPT1 by phenylarsonic acids.Dalton transactions (Cambridge, England : 2003) · 2026Article
- Are you having a LaPh? Diverse roles of Labile Phosphorylation in mammalian cells.Biochemical Society transactions · 2025Review
- Histidine Phosphorylation: Protein Kinases and Phosphatases.International journal of molecular sciences · 2024Review
- A salt bridge of the C-terminal carboxyl group regulates PHPT1 substrate affinity and catalytic activity.Protein science : a publication of the Protein Society · 2024Article
- Derivatives of the Fungal Natural Product Illudalic Acid Inhibit the Activity of Protein Histidine Phosphatase PHPT1.ChemMedChem · 2023Article
- Inhibitor Screen Identifies Covalent Inhibitors of the Protein Histidine Phosphatase PHPT1.ACS medicinal chemistry letters · 2022Article
- [Roles of Histidine Kinases and Histidine Phosphatases in Cancer].Zhongguo fei ai za zhi = Chinese journal of lung cancer · 2021Review
- Synthesis and Evaluation of Non-Hydrolyzable Phospho-Lysine Peptide Mimics.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Immunohistochemistry (IHC): Chromogenic Detection of 3-Phosphohistidine Proteins in Formaldehyde-Fixed, Frozen Mouse Liver Tissue Sections.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Strong anion exchange-mediated phosphoproteomics reveals extensive human non-canonical phosphorylation.The EMBO journal · 2019Article
- Microcystin Levels in Selected Cyanobacteria Exposed to Varying Salinity.Journal of water resource and protection · 2019Article
- Natural Products Containing 'Rare' Organophosphorus Functional Groups.Molecules (Basel, Switzerland) · 2019Review
- The actions of NME1/NDPK-A and NME2/NDPK-B as protein kinases.Laboratory investigation; a journal of technical methods and pathology · 2018Review
- Structural and activity characterization of human PHPT1 after oxidative modification.Scientific reports · 2016Article
- Phosphoproteomics in the Age of Rapid and Deep Proteome Profiling.Analytical chemistry · 2016Review
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3 authors at 1 institution in 1 country.
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Abstract
backgroundPhosphohistidine phosphatase 1 (PHPT1), also named protein histidine phosphatase (PHP), is a eukaryotic enzyme dephosphorylating proteins and peptides that are phosphorylated on a histidine residue. A preliminary finding that histone H1, which lacks histidine, was phosphorylated by phosphoramidate and dephosphorylated by PHPT1 prompted the present investigation.
methodsHistone H1 and polylysine were phosphorylated at a low concentration (3.9 mM) of phosphoramidate. Their dephosphorylation by recombinant human PHPT1 was investigated by using a DEAE-Sepharose spin column technique earlier developed by us for studies on basic phosphoproteins and phosphopeptides. Determination of protein-bound, acid-labile phosphate was performed by a malachite green method. Mass spectrometry (MS) was used to investigate the occurrence of N-ε-phospholysine residues in a phosphorylated histone H1.2 preparation, and to measure the activity of PHPT1 against free N-ω-phosphoarginine.
resultsHistone H1.2, which lacks histidine, was phosphorylated by phosphoramidate on several lysine residues, as shown by MS. PHPT1 was shown to dephosphorylate phosphohistone H1 at a rate similar to that previously described for the dephosphorylation of phosphohistidine-containing peptides. In addition, phosphopolylysine was an equally good substrate for PHPT1. However, no dephosphorylation of free phosphoarginine by PHPT1 could be detected.
conclusionThe finding that PHPT1 can dephosphorylate phospholysine in chemically phosphorylated histone H1 and polylysine demonstrates a broader specificity for this enzyme than known so far.
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