PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2535870-5 1989 During theophylline therapy, erythrocyte pyridoxal kinase levels increased nearly twofold from an initial mean level of 24.2 +/- 4.0 (+/- SD) nmol to 46.9 +/- 7.3 nmol pyridoxal-5"-phosphate per gram of hemoglobin per hour. Pyridoxal Phosphate 168-190 pyridoxal kinase Homo sapiens 41-57 31578392-1 2019 In eukaryotes, pyridoxal kinase (PDXK) acts in vitamin B6 salvage pathway to produce pyridoxal 5"-phosphate (PLP), the active form of the vitamin, which is implicated in numerous crucial metabolic reactions. Pyridoxal Phosphate 85-107 pyridoxal kinase Homo sapiens 15-31 474471-1 1979 The effects of pyridoxine and pyridoxal 5-phosphate (PLP) administration on pyridoxine kinase (PnK) and asparate aminotransferase (EGOT), a PLP-dependent enzyme, were studied in human red cells separated into young and old populations by density centrifugation. Pyridoxal Phosphate 53-56 pyridoxal kinase Homo sapiens 76-93 33555078-2 2021 In contrast, enzymes with pyridoxal kinase activity (PLK) produce pyridoxal phosphate (vitamin B6), an essential cofactor for various biochemical reactions. Pyridoxal Phosphate 66-85 pyridoxal kinase Homo sapiens 26-42 31935373-2 2020 We performed a CRISPR/Cas9 functional genomic screen targeting metabolic enzymes and identified PDXK-an enzyme that produces pyridoxal phosphate (PLP) from vitamin B6-as an acute myeloid leukemia (AML)-selective dependency. Pyridoxal Phosphate 125-144 pyridoxal kinase Homo sapiens 96-100 31935373-2 2020 We performed a CRISPR/Cas9 functional genomic screen targeting metabolic enzymes and identified PDXK-an enzyme that produces pyridoxal phosphate (PLP) from vitamin B6-as an acute myeloid leukemia (AML)-selective dependency. Pyridoxal Phosphate 146-149 pyridoxal kinase Homo sapiens 96-100 33318193-4 2020 Here, we report the crystal structure of the central metabolic enzyme pyridoxal kinase (PDXK), which catalyzes the production of the active form of vitamin B6 (also known as pyridoxal 5"-phosphate [PLP]), in complex with artesunate at 2.4-A resolution. Pyridoxal Phosphate 174-196 pyridoxal kinase Homo sapiens 70-86 33318193-4 2020 Here, we report the crystal structure of the central metabolic enzyme pyridoxal kinase (PDXK), which catalyzes the production of the active form of vitamin B6 (also known as pyridoxal 5"-phosphate [PLP]), in complex with artesunate at 2.4-A resolution. Pyridoxal Phosphate 174-196 pyridoxal kinase Homo sapiens 88-92 32522499-1 2020 PDXK encodes for a pyridoxal kinase, which converts inactive B6 vitamers to the active cofactor pyridoxal 5"-phosphate (PLP). Pyridoxal Phosphate 96-118 pyridoxal kinase Homo sapiens 0-4 32522499-1 2020 PDXK encodes for a pyridoxal kinase, which converts inactive B6 vitamers to the active cofactor pyridoxal 5"-phosphate (PLP). Pyridoxal Phosphate 120-123 pyridoxal kinase Homo sapiens 0-4 32610066-3 2020 demonstrate that pyridoxal kinase promotes vitamin B6 phosphorylation, producing the active form pyridoxal 5"-phosphate, which regulates two key metabolic enzymes required for acute myeloid leukemia (AML) cell growth. Pyridoxal Phosphate 97-119 pyridoxal kinase Homo sapiens 17-33 32105687-1 2020 The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5"-phosphate (PLP) using ATP as the co-factor. Pyridoxal Phosphate 76-98 pyridoxal kinase Homo sapiens 29-33 32105687-1 2020 The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5"-phosphate (PLP) using ATP as the co-factor. Pyridoxal Phosphate 100-103 pyridoxal kinase Homo sapiens 29-33 31578392-1 2019 In eukaryotes, pyridoxal kinase (PDXK) acts in vitamin B6 salvage pathway to produce pyridoxal 5"-phosphate (PLP), the active form of the vitamin, which is implicated in numerous crucial metabolic reactions. Pyridoxal Phosphate 85-107 pyridoxal kinase Homo sapiens 33-37 28716709-1 2017 Pyridoxal kinase is a key enzyme for the biosynthesis of pyridoxal 5"-phosphate. Pyridoxal Phosphate 57-79 pyridoxal kinase Homo sapiens 0-16 31187503-0 2019 PDXK mutations cause polyneuropathy responsive to pyridoxal 5"-phosphate supplementation. Pyridoxal Phosphate 50-72 pyridoxal kinase Homo sapiens 0-4 31187503-9 2019 Low PDXK ATP binding resulted in decreased erythrocyte PDXK activity and low pyridoxal 5"-phosphate (PLP) concentrations. Pyridoxal Phosphate 77-99 pyridoxal kinase Homo sapiens 4-8 17696614-5 2007 The most potent novel GCR suppressor identified is BUD16, the gene coding for yeast pyridoxal kinase (Pdxk), a key enzyme in the metabolism of pyridoxal 5" phosphate (PLP), the biologically active form of vitamin B6. Pyridoxal Phosphate 143-165 pyridoxal kinase Homo sapiens 102-106 24899377-3 2015 Pyridoxal kinase inhibition by THI has been suggested, but not demonstrated, as a mode of action as it leads to lowered levels of pyridoxal-5"-phosphate, which are known to cause lymphopenia. Pyridoxal Phosphate 130-152 pyridoxal kinase Homo sapiens 0-16 24899377-5 2015 Interestingly, sphingosine-1-phosphate lyase activity depends on pyridoxal-5"-phosphate, which in turn is provided by pyridoxal kinase. Pyridoxal Phosphate 65-87 pyridoxal kinase Homo sapiens 118-134 23860900-1 2013 Pyridoxal 5"-phosphate is the active form of vitamin B6 and its deficiency is directly related with several human disorders, which make human pyridoxal kinase (hPLK) an important pharmacologic target. Pyridoxal Phosphate 0-22 pyridoxal kinase Homo sapiens 142-158 22879864-2 2012 The neurotoxic effects of some of these compounds, including theophylline and ginkgotoxin, have been traced to their inhibitory activity against human pyridoxal kinase (hPL kinase), resulting in deficiency of the active cofactor form of vitamin B6, pyridoxal 5"-phosphate (PLP). Pyridoxal Phosphate 249-271 pyridoxal kinase Homo sapiens 151-167 19351586-1 2009 Pyridoxal kinase catalyzes the phosphorylation of pyridoxal (PL) to pyridoxal 5"-phosphate (PLP). Pyridoxal Phosphate 68-90 pyridoxal kinase Homo sapiens 0-16 17696614-5 2007 The most potent novel GCR suppressor identified is BUD16, the gene coding for yeast pyridoxal kinase (Pdxk), a key enzyme in the metabolism of pyridoxal 5" phosphate (PLP), the biologically active form of vitamin B6. Pyridoxal Phosphate 167-170 pyridoxal kinase Homo sapiens 102-106 16600635-1 2006 Pyridoxal kinase, a member of the ribokinase superfamily, catalyzes the ATP-dependent phosphorylation reaction of vitamin B6 and is an essential enzyme in the formation of pyridoxal-5"-phosphate, a key cofactor for over 100 enzymes. Pyridoxal Phosphate 172-194 pyridoxal kinase Homo sapiens 0-16 15381280-2 2004 GAD isoforms (GAD65 and GAD67) differ substantially in their interactions with cofactor pyridoxal 5"-phosphate, which is catalyzed by pyridoxal kinase (PLK). Pyridoxal Phosphate 88-110 pyridoxal kinase Homo sapiens 134-150 15820755-1 2005 Pyridoxal kinase (PK) catalyses the phosphorylation of vitamin B6 to pyridoxal-5"-phosphate (PLP). Pyridoxal Phosphate 69-91 pyridoxal kinase Homo sapiens 0-16 15820755-1 2005 Pyridoxal kinase (PK) catalyses the phosphorylation of vitamin B6 to pyridoxal-5"-phosphate (PLP). Pyridoxal Phosphate 69-91 pyridoxal kinase Homo sapiens 18-20 15820755-1 2005 Pyridoxal kinase (PK) catalyses the phosphorylation of vitamin B6 to pyridoxal-5"-phosphate (PLP). Pyridoxal Phosphate 93-96 pyridoxal kinase Homo sapiens 0-16 15820755-1 2005 Pyridoxal kinase (PK) catalyses the phosphorylation of vitamin B6 to pyridoxal-5"-phosphate (PLP). Pyridoxal Phosphate 93-96 pyridoxal kinase Homo sapiens 18-20 15381280-2 2004 GAD isoforms (GAD65 and GAD67) differ substantially in their interactions with cofactor pyridoxal 5"-phosphate, which is catalyzed by pyridoxal kinase (PLK). Pyridoxal Phosphate 88-110 pyridoxal kinase Homo sapiens 152-155 11983425-10 2002 The order of affinity of PK for different analogues is: pyridoxal-oxime>pyridoxine>pyridoxamine>pyridoxal>pyridoxal phosphate. Pyridoxal Phosphate 118-137 pyridoxal kinase Homo sapiens 25-27 7778760-1 1995 We have developed an assay for pyridoxal kinase which takes advantage of the intense fluorescence yield of the oxime of pyridoxal or pyridoxal-5"-phosphate and the substantial difference in the rates of formation of these two oximes. Pyridoxal Phosphate 133-155 pyridoxal kinase Homo sapiens 31-47 2231024-2 1990 Total erythrocyte pyridoxal kinase levels increased during 15 wk of theophylline treatment from a mean initial activity of 19.23 +/- 5.03 (mean +/- SD) to 62.64 +/- 11.59 nmol pyridoxal-5"-phosphate formed/(g hemoglobin.h). Pyridoxal Phosphate 176-198 pyridoxal kinase Homo sapiens 18-34 35050500-2 2022 Here, the non-coenzyme action of thiamine on the major mammalian producers of pyridoxal-5"-phosphate (PLP), such as pyridoxal kinase (PdxK) and pyridoxine 5"-phosphate oxidase (PNPO), is characterized. Pyridoxal Phosphate 78-100 pyridoxal kinase Homo sapiens 116-132 35050500-2 2022 Here, the non-coenzyme action of thiamine on the major mammalian producers of pyridoxal-5"-phosphate (PLP), such as pyridoxal kinase (PdxK) and pyridoxine 5"-phosphate oxidase (PNPO), is characterized. Pyridoxal Phosphate 78-100 pyridoxal kinase Homo sapiens 134-138