Disease relevance of phosphohistidine

• Phosphoenolypyruvate synthetase of Escherichia coli: molecular weight, subunit composition, and identification of phosphohistidine in phosphoenzyme intermediate [1].

High impact information on phosphohistidine

• With thrombin stimulation, the kinetics of phosphohistidine appearance and disappearance of P-selectin are very rapid [2].
• We now establish that phosphorylation following platelet activation with thrombin or collagen generates phosphohistidine at histidines on the cytoplasmic tail of P-selectin [2].
• The pH-stability profile of the phosphoenzyme intermediate was consistent with phosphohistidine and the only radioactive amino acid found after alkaline hydrolysis was phosphohistidine [3].
• Catalytic mechanism of the phospholipase D superfamily proceeds via a covalent phosphohistidine intermediate [3].
• Coupling between the two remote active sites is facilitated by two conformational states of the phosphohistidine domain [4].

Chemical compound and disease context of phosphohistidine

• Structural consequences of histidine phosphorylation: NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli [5].

Biological context of phosphohistidine

• Several lines of evidence, including identification of 3-phosphohistidine in alkaline digests of the phosphoenzyme, indicate that a histidyl residue is the site of phosphorylation [1].
• The amino acid sequence of the phosphohistidine peptide has been determined to be: His-Gly-Gln-Gly-Ala-Trp-Asn-Lys [6].
• Each monomer has an extended configuration with the phosphohistidine and heat-stable phospho carrier protein-binding domains clearly separated from the C-terminal dimerization and PEP-binding region [7].
• The wild-type and one of the mutant SpoOA proteins were purified and shown to be competent to accept phosphoryl groups from a phosphohistidine within a bacterial signal transduction kinase (CheA) [8].
• The "catalytic" site is very acid labile and has been suggested by different workers to contain either phosphohistidine or an acyl phosphate group [9].

Anatomical context of phosphohistidine

• 6-Phospholysine phosphatase (30 kDa) and 3-phosphohistidine/6-phospholysine phosphatase (150 kDa) were purified partially from rat brain cytosol [10].
• The formation of phosphohistidine residues in proteins has been discovered in prokaryotic organisms as well as in eukaryotic cells [11].
• The isolation and characterization of an active site phosphohistidine peptide from human erythrocyte bisphosphoglycerate synthase [12].
• We have shown that proteins within apically enriched fractions of human nasal respiratory epithelium vary their phosphohistidine content with ambient [Cl(-)] and other anion concentrations [13].

Associations of phosphohistidine with other chemical compounds

• The antibody also bound ATP citrate lyase; this enzyme lacks phosphotyrosine but contains phosphohistidine, which is similar structurally to phosphotyrosine [14].
• Histidine 167 is the phosphate acceptor in glucose-6-phosphatase-beta forming a phosphohistidine enzyme intermediate during catalysis [15].
• D-Lactate inhibits the phosphatase activity that removes phosphoaspartate groups from the receiver module in ArcB, and the associated increase in phosphorylation of this module leads to an activation of transphosphorylation of subsequently added phosphohistidine groups on ArcB to the receiver module of ArcA [16].
• Phosphorus-31 nuclear magnetic resonance study of the active site phosphohistidine and regulatory phosphoserine residues of rat liver ATP-citrate lyase [9].
• Pyridine and hydroxylamine-catalyzed hydrolysis of E-P gave second-order rate constants consistent with published values for phosphohistidine [17].

Gene context of phosphohistidine

• Identification of YPD1, a gene of Candida albicans which encodes a two-component phosphohistidine intermediate protein [18].
• The catalytic center of glucose-6-phosphatase. HIS176 is the nucleophile forming the phosphohistidine-enzyme intermediate during catalysis [19].
• Immunoprecipitated 32P-labeled isocitrate lyase was subjected to alkaline hydrolysis, mixed with chemically synthesized phosphohistidine standards, and analyzed by anion exchange chromatography [20].
• In addition to its activity on phosphotyrosine and phosphohistidine substrates, Tdp1 also possesses a limited DNA and RNA 3'-exonuclease activity in which a single nucleoside is removed from the 3'-hydroxyl end of the substrate [21].
• Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium [22].

Analytical, diagnostic and therapeutic context of phosphohistidine

• NaDodSO4--polyacrylamide gel electrophoresis confirms acid lability, and high-pressure liquid chromatography of protein hydrolysates yields phosphohistidine [23].
• Phosphohistidine analysis using reversed-phase thin-layer chromatography [24].
• Possibly, the lyophilization and preparation of solutions for NMR analysis resulted in a certain amount of hydrolysis of phosphohistidine, particularly with the less stable 1- and 1,3-forms (5, 6) [25].

References