Pub. Date : 2015 Mar
PMID : 25574816
13 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Phosphohistidine phosphatase 1 (PHPT1) also dephosphorylates phospholysine of chemically phosphorylated histone H1 and polylysine. | phospholysine | phosphohistidine phosphatase 1 | Homo sapiens |
| 2 | Phosphohistidine phosphatase 1 (PHPT1) also dephosphorylates phospholysine of chemically phosphorylated histone H1 and polylysine. | phospholysine | phosphohistidine phosphatase 1 | Homo sapiens |
| 3 | BACKGROUND: Phosphohistidine phosphatase 1 (PHPT1), also named protein histidine phosphatase (PHP), is a eukaryotic enzyme dephosphorylating proteins and peptides that are phosphorylated on a histidine residue. | Histidine | phosphohistidine phosphatase 1 | Homo sapiens |
| 4 | BACKGROUND: Phosphohistidine phosphatase 1 (PHPT1), also named protein histidine phosphatase (PHP), is a eukaryotic enzyme dephosphorylating proteins and peptides that are phosphorylated on a histidine residue. | Histidine | phosphohistidine phosphatase 1 | Homo sapiens |
| 5 | 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. | deae-sepharose | phosphohistidine phosphatase 1 | Homo sapiens |
| 6 | Mass spectrometry (MS) was used to investigate the occurrence of N-epsilon-phospholysine residues in a phosphorylated histone H1.2 preparation, and to measure the activity of PHPT1 against free N-omega-phosphoarginine. | n-omega-phosphoarginine | phosphohistidine phosphatase 1 | Homo sapiens |
| 7 | RESULTS: Histone 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. | Histidine | phosphohistidine phosphatase 1 | Homo sapiens |
| 8 | RESULTS: Histone 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. | phosphoramidic acid | phosphohistidine phosphatase 1 | Homo sapiens |
| 9 | RESULTS: Histone 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. | Lysine | phosphohistidine phosphatase 1 | Homo sapiens |
| 10 | RESULTS: Histone 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. | phosphohistidine | phosphohistidine phosphatase 1 | Homo sapiens |
| 11 | In addition, phosphopolylysine was an equally good substrate for PHPT1. | phosphopolylysine | phosphohistidine phosphatase 1 | Homo sapiens |
| 12 | CONCLUSION: The finding that PHPT1 can dephosphorylate phospholysine in chemically phosphorylated histone H1 and polylysine demonstrates a broader specificity for this enzyme than known so far. | phospholysine | phosphohistidine phosphatase 1 | Homo sapiens |
| 13 | CONCLUSION: The finding that PHPT1 can dephosphorylate phospholysine in chemically phosphorylated histone H1 and polylysine demonstrates a broader specificity for this enzyme than known so far. | Polylysine | phosphohistidine phosphatase 1 | Homo sapiens |