Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase.

@article{Ek2002IdentificationAC,
  title={Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase.},
  author={Pia Ek and Gunilla Pettersson and Bo Ek and Feng Gong and Jin-ping Li and Orjan Zetterqvist},
  journal={European journal of biochemistry},
  year={2002},
  volume={269 20},
  pages={
          5016-23
        }
}
Protein histidine phosphorylation in eukaryotes has been sparsely studied compared to protein serine/threonine and tyrosine phosphorylation. In an attempt to rectify this by probing porcine liver cytosol with the phosphohistidine-containing peptide succinyl-Ala-His(P)-Pro-Phe-p-nitroanilide (phosphopeptide I), we observed a phosphatase activity that was insensitive towards okadaic acid and EDTA. This suggested the existence of a phosphohistidine phosphatase different from protein phosphatase 1… 
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References

SHOWING 1-10 OF 35 REFERENCES

Identification of phosphohistidine in proteins and purification of protein-histidine kinases.

Bovine liver phosphoamidase as a protein histidine/lysine phosphatase.

A 13-kDa phosphoamidase was isolated as a single band on SDS-PAGE from bovine liver and dephosphorylated succinic thiokinase and nucleoside diphosphate kinase autophosphorylation at His residues, indicating that it works as a protein histidine phosphatase.

Purification of a protein histidine kinase from the yeast Saccharomyces cerevisiae. The first member of this class of protein kinases.

Phosphorylation and dephosphorylation of histidine residues in proteins.

This minireview briefly summarizes the extensive knowledge of the key mechanisms and functions of phosphohistidine in bacteria and describes the still limited, yet increasing, data from homologs of the bacterial two-component system.

Protein phosphatases 1, 2A, and 2C are protein histidine phosphatases.

Cloning and expression of a human ATP-citrate lyase cDNA.

Results are consistent with the pattern of earlier observations of the significance of the histidine residue in catalysis of the human ATP-citrate lyase.

Synthesis and characterization of histidine‐phosphorylated peptides

Methods for the synthesis and analysis of phosphohistidine‐containing peptides are described, a prerequisite for the investigation of the role of this posttranslational modification in cellular processes.

Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium.

The X-ray structures of phosphorylated NDP kinase and of previously determined complexes with nucleosid diphosphates provide a basis for modeling the Michaelis complex with a nucleoside triphosphate, the transition state of the phosphate transfer reaction in which the gamma-ph phosphate is pentacoordinated.

Protein kinases and phosphatases that act on histidine, lysine, or arginine residues in eukaryotic proteins: a possible regulator of the mitogen-activated protein kinase cascade.

Molecular Characterization of an Apical Early Endosomal Glycoprotein from Developing Rat Intestinal Epithelial Cells (*)

The major form of this protein in intestinal epithelial cells has a molecular mass of 55-60 kDa, which is significantly smaller than the size predicted from the cDNA sequence, suggesting that the protein is synthesized as a large precursor and processed to the smaller form.