PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19825182-3 2009 DOHH activity is inhibited by two clinically used drugs, the topical fungicide ciclopirox and the systemic medicinal iron chelator deferiprone. Iron 117-121 deoxyhypusine hydroxylase Homo sapiens 0-4 23943044-7 2013 This pre-selective step of parasitic eradication will be used further for a test of the Malaria Box with a potential in iron chelating capacity to inhibit deoxyhypusine hydroxylase (DOHH) from P. falciparum and vivax. Iron 120-124 deoxyhypusine hydroxylase Homo sapiens 155-180 19706422-2 2009 Recombinant human deoxyhypusine hydroxylase (hDOHH) has been reported to have oxygen- and iron-dependent activity, an estimated iron/holoprotein stoichiometry of 2, and a visible band at 630 nm responsible for the blue color of the as-isolated protein. Iron 90-94 deoxyhypusine hydroxylase Homo sapiens 18-43 19706422-2 2009 Recombinant human deoxyhypusine hydroxylase (hDOHH) has been reported to have oxygen- and iron-dependent activity, an estimated iron/holoprotein stoichiometry of 2, and a visible band at 630 nm responsible for the blue color of the as-isolated protein. Iron 90-94 deoxyhypusine hydroxylase Homo sapiens 45-50 16533814-5 2006 The purified human recombinant DOHH was a mixture of active holoenzyme containing 2 mol of iron/mol of DOHH and inactive metal-free apoenzyme. Iron 91-95 deoxyhypusine hydroxylase Homo sapiens 31-35 16533814-7 2006 The DOHH apoenzyme exhibited markedly reduced levels of iron and activity. Iron 56-60 deoxyhypusine hydroxylase Homo sapiens 4-8 16533814-13 2006 Furthermore, the iron to DOHH stoichiometry and dependence of iron binding on each of the four conserved His-Glu motifs suggest a binuclear iron mediated reaction mechanism, distinct from that of other Fe(II)-dependent protein hydroxylases, such as prolyl 4-hydroxylase or lysyl hydroxylases. Iron 17-21 deoxyhypusine hydroxylase Homo sapiens 25-29 16371467-10 2006 However, metal coordination sites composed of four strictly conserved histidine-glutamate sequences were identified, suggesting that DOHH enzymes have convergently evolved an iron-dependent hydroxylation mechanism. Iron 175-179 deoxyhypusine hydroxylase Homo sapiens 133-137 24843120-3 2014 Here, we show that PCBP1 and PCBP2 also deliver iron to deoxyhypusine hydroxylase (DOHH), the dinuclear iron enzyme required for hypusine modification of the translation factor eukaryotic initiation factor 5A. Iron 48-52 deoxyhypusine hydroxylase Homo sapiens 56-81 24843120-3 2014 Here, we show that PCBP1 and PCBP2 also deliver iron to deoxyhypusine hydroxylase (DOHH), the dinuclear iron enzyme required for hypusine modification of the translation factor eukaryotic initiation factor 5A. Iron 48-52 deoxyhypusine hydroxylase Homo sapiens 83-87 24843120-3 2014 Here, we show that PCBP1 and PCBP2 also deliver iron to deoxyhypusine hydroxylase (DOHH), the dinuclear iron enzyme required for hypusine modification of the translation factor eukaryotic initiation factor 5A. Iron 104-108 deoxyhypusine hydroxylase Homo sapiens 56-81 24843120-3 2014 Here, we show that PCBP1 and PCBP2 also deliver iron to deoxyhypusine hydroxylase (DOHH), the dinuclear iron enzyme required for hypusine modification of the translation factor eukaryotic initiation factor 5A. Iron 104-108 deoxyhypusine hydroxylase Homo sapiens 83-87 24843120-6 2014 PCBP1 bound to DOHH in iron-treated cells but not in control or iron-deficient cells. Iron 23-27 deoxyhypusine hydroxylase Homo sapiens 15-19 23943044-7 2013 This pre-selective step of parasitic eradication will be used further for a test of the Malaria Box with a potential in iron chelating capacity to inhibit deoxyhypusine hydroxylase (DOHH) from P. falciparum and vivax. Iron 120-124 deoxyhypusine hydroxylase Homo sapiens 182-186 23943044-8 2013 DOHH, a metalloprotein which consists of ferrous iron and catalyzes the second step of the posttranslational modification at a specific lysine in eukaryotic initiation factor 5A (EIF-5A) to hypusine. Iron 49-53 deoxyhypusine hydroxylase Homo sapiens 0-4