PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29090276-1 2017 BACKGROUND: Hexokinase and glucokinase enzymes are ubiquitously expressed and use ATP and ADP as substrates in mammalian systems and a variety of polyphosphate substrates and/or ATP in some eukaryotic and microbial systems. Adenosine Triphosphate 82-85 glucokinase Homo sapiens 27-38 29090276-1 2017 BACKGROUND: Hexokinase and glucokinase enzymes are ubiquitously expressed and use ATP and ADP as substrates in mammalian systems and a variety of polyphosphate substrates and/or ATP in some eukaryotic and microbial systems. Adenosine Triphosphate 178-181 glucokinase Homo sapiens 27-38 29090276-5 2017 RESULTS: A novel mammalian glucokinase, highly responsive to hexametaphosphate (HMP) but not ATP or ADP as a phosphoryl donor is present in the nuclei of mammalian hepatocytes. Adenosine Triphosphate 93-96 glucokinase Homo sapiens 27-38 29090276-9 2017 CONCLUSIONS: We report the discovery of a polyphosphate-dependent enzyme system in mammalian cells with kinetics similar to established ATP-dependent glucokinase, also known to have a nuclear location. Adenosine Triphosphate 136-139 glucokinase Homo sapiens 150-161 26028562-4 2015 A high expression level of glucokinase enabled efficient glucose phosphorylation, increasing the ATP/ADP ratio along with stimulation of insulin secretion in the physiological glucose concentration range. Adenosine Triphosphate 97-100 glucokinase Homo sapiens 27-38 22107947-1 2012 Glucokinase catalyzes the ATP-dependent phosphorylation of glucose, a chemical transformation that represents the rate-limiting step of glycolytic metabolism in the liver and pancreas. Adenosine Triphosphate 26-29 glucokinase Homo sapiens 0-11 22829728-2 2012 There exist four different forms of HKs namely HK-I, HK-II, HK-III and HK-IV and all of them share a common ATP binding site core surrounded by more variable sequence that determine substrate affinities. Adenosine Triphosphate 108-111 glucokinase Homo sapiens 71-76 22101819-1 2011 Glucokinase (GK) catalyses the formation of glucose 6-phosphate from glucose and ATP. Adenosine Triphosphate 81-84 glucokinase Homo sapiens 0-11 22101819-1 2011 Glucokinase (GK) catalyses the formation of glucose 6-phosphate from glucose and ATP. Adenosine Triphosphate 81-84 glucokinase Homo sapiens 13-15 21420961-0 2011 Crystal structure of E339K mutated human glucokinase reveals changes in the ATP binding site. Adenosine Triphosphate 76-79 glucokinase Homo sapiens 41-52 19617908-6 2009 QM/MM calculations were further used to study the role of Lys169 in the catalytic mechanism of the glucose phosphorylation and we found that Lys169 enhances the binding of GK with both ATP and glucose by serving as a bridge between ATP and glucose. Adenosine Triphosphate 185-188 glucokinase Homo sapiens 172-174 19617908-6 2009 QM/MM calculations were further used to study the role of Lys169 in the catalytic mechanism of the glucose phosphorylation and we found that Lys169 enhances the binding of GK with both ATP and glucose by serving as a bridge between ATP and glucose. Adenosine Triphosphate 232-235 glucokinase Homo sapiens 172-174 19459610-11 2009 Additionally, a perturbation of the GKA binding kinetic parameters after preequilibration of closed GK with an ATP analogue suggested a local rearrangement of the allosteric site upon nucleotide binding. Adenosine Triphosphate 111-114 glucokinase Homo sapiens 36-38 18298419-2 2008 We report here the first known case caused by a homozygous nonsense mutation (Y61X) in the glucokinase gene (GCK) that introduces a premature stop codon, generating a truncated protein that is predicted to be completely inactive as it lacks both the glucose- and the adenosine triphosphate-binding sites. Adenosine Triphosphate 267-289 glucokinase Homo sapiens 91-102 18298419-2 2008 We report here the first known case caused by a homozygous nonsense mutation (Y61X) in the glucokinase gene (GCK) that introduces a premature stop codon, generating a truncated protein that is predicted to be completely inactive as it lacks both the glucose- and the adenosine triphosphate-binding sites. Adenosine Triphosphate 267-289 glucokinase Homo sapiens 109-112 18199594-11 2008 In summary, mechanisms downstream of AMPK activation, involving phosphorylation of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase and GKRP are involved in the ATP-independent inhibition of glucose-induced glucokinase translocation by AICAR in hepatocytes. Adenosine Triphosphate 165-168 glucokinase Homo sapiens 211-222 17260972-5 2007 The rates of conformational transitions of free and GK complexed with sugar are slow and during catalysis are most likely affected by ATP binding, phosphate transfer, and product release steps to allow the kcat to be 60 s-1. Adenosine Triphosphate 134-137 glucokinase Homo sapiens 52-54 17260972-6 2007 The ATP analogue PNP-AMP binds to free GK (super-open) and GK-glucose (open) complexes with comparable affinities (Kd = 0.23 +/- 0.02 and 0.19 +/- 0.08 mM, respectively). Adenosine Triphosphate 4-7 glucokinase Homo sapiens 39-41 17986831-5 2007 Autosomal dominant mutations in the genes encoding glucokinase (GCK) and glutamate dehydrogenase (GLUD1) lead to inappropriate insulin secretion by increasing the ATP/ADP ratio in the Beta-cells. Adenosine Triphosphate 163-166 glucokinase Homo sapiens 51-62 17986831-5 2007 Autosomal dominant mutations in the genes encoding glucokinase (GCK) and glutamate dehydrogenase (GLUD1) lead to inappropriate insulin secretion by increasing the ATP/ADP ratio in the Beta-cells. Adenosine Triphosphate 163-166 glucokinase Homo sapiens 64-67 15752705-0 2005 Identification and characterization of the ATP-binding site in human pancreatic glucokinase. Adenosine Triphosphate 43-46 glucokinase Homo sapiens 80-91 15752705-3 2005 Human pancreatic glucokinase mutants were designed based upon these models and on ATPase domain sequence conservation to identify and characterize potential glucose and ATP-binding sites. Adenosine Triphosphate 82-85 glucokinase Homo sapiens 17-28 15752705-6 2005 Results suggest a role for Asp78, Thr82, Gly227, Thr228, and Ser336 in ATP binding and indicate these residues are essential for glucose phosphorylation by human pancreatic glucokinase. Adenosine Triphosphate 71-74 glucokinase Homo sapiens 173-184 14688272-4 2004 Exposure of cells with enhanced GK activity to 20 mm glucose accelerated glycolysis, but reduced cellular NAD(P)H and ATP, caused accumulation of intracellular reactive oxygen species (ROS) and oxidative damage to mitochondria and DNA, and promoted apoptotic cell death. Adenosine Triphosphate 118-121 glucokinase Homo sapiens 32-34 14975750-2 2004 The ubiquitous mammalian ATP-dependent hexokinases I-III and hexokinase IV, also termed glucokinase, initiate the process by phosphorylating glucose to glucose-6-phosphate. Adenosine Triphosphate 25-28 glucokinase Homo sapiens 88-99 14975750-3 2004 Despite glycolysis having been studied extensively for over 70 years and the last new mammalian ATP-dependent hexokinase isotype having been described in the 1960s, we report here the biochemical characterization of a recombinant ADP-dependent glucokinase cloned from a full-length Mus musculus cDNA, identified by sequence analysis. Adenosine Triphosphate 96-99 glucokinase Homo sapiens 244-255 11551839-5 2001 In contrast, neuroendocrine hypothalamic responses in glucoresponsive and glucose-sensitive neurons (either excitation or inhibition, respectively) to physiological changes in glucose concentration appear to depend on glucokinase; neuroendocrine responses also depend on K-ATP channels, although the role of ATP itself is less clear. Adenosine Triphosphate 273-276 glucokinase Homo sapiens 218-229 11594461-1 2001 Glucokinase catalyzes phosphoryl group transfer from ATP to glucose to form glucose-6-phosphate in the first step of cellular metabolism. Adenosine Triphosphate 53-56 glucokinase Homo sapiens 0-11 11594461-2 2001 While the location of the ATP-binding site of glucokinase was proposed recently, limited information exists on its conformation or the key amino acids involved in substrate binding. Adenosine Triphosphate 26-29 glucokinase Homo sapiens 46-57 10480597-0 1999 Structural model of human glucokinase in complex with glucose and ATP: implications for the mutants that cause hypo- and hyperglycemia. Adenosine Triphosphate 66-69 glucokinase Homo sapiens 26-37 10480597-4 1999 Glucokinase was modeled with both its substrates, glucose and MgATP, to understand the effect of mutations. Adenosine Triphosphate 62-67 glucokinase Homo sapiens 0-11 9684361-8 1998 Glucokinase activity was optimal between pH 7.5 and 8.5, preferred ATP as the phosphate donor (K(m) = 0.223 mM) and exhibited low activity with GTP or UTP. Adenosine Triphosphate 67-70 glucokinase Homo sapiens 0-11 9275185-7 1997 Interestingly, deletion of amino acids 353-835 in the putative C-terminal regulatory region, or mutation of Lys-35 in the putative ATP-binding domain, markedly reduced the ability of GLK to activate JNK. Adenosine Triphosphate 131-134 glucokinase Homo sapiens 183-186 8639629-0 1996 Initial rate and equilibrium isotope exchange studies on the ATP-dependent activity of polyphosphate Glucokinase from Propionibacterium shermanii. Adenosine Triphosphate 61-64 glucokinase Homo sapiens 101-112 8639629-1 1996 Polyphosphate glucokinase [EC 2.7.1.63] catalyzes the phosphorylation of glucose using either inorganic polyphosphate [poly(P)] or ATP as the phosphoryl donor. Adenosine Triphosphate 131-134 glucokinase Homo sapiens 14-25 7619052-9 1995 of GK, a decrease in the ATP-binding affinity or stability of the mutated enzyme may also contribute to a reduction of GK activity in individuals with GK-MODY. Adenosine Triphosphate 25-28 glucokinase Homo sapiens 3-5 7619052-9 1995 of GK, a decrease in the ATP-binding affinity or stability of the mutated enzyme may also contribute to a reduction of GK activity in individuals with GK-MODY. Adenosine Triphosphate 25-28 glucokinase Homo sapiens 119-121 2582618-2 1989 Magnesium participates as an Mg.ATP complex in a reaction catalyzed by glucokinase (EC 2.7.1.2) coupled to an NADP+-dependent glucose-6-phosphate dehydrogenase (EC 1.1.1.49) reaction. Adenosine Triphosphate 32-35 glucokinase Homo sapiens 71-82 16666820-7 1989 The cytoplasmic phosphofructokinase and fructokinase in plants were fairly nonselective for nucleotide triphosphates (NTP) but glucokinase definitely favored ATP. Adenosine Triphosphate 158-161 glucokinase Homo sapiens 127-138 3663182-2 1987 When ATP, the normal phosphate donor for hexokinase D ("glucokinase"), is replaced by ITP, the positive co-operativity with respect to glucose disappears. Adenosine Triphosphate 5-8 glucokinase Homo sapiens 56-68 196677-4 1977 Solubilizations by ATP and glucose-6-phosphate differ in their sensitivity to temperature changes; they are relatively specific for glucokinase as compared to solubilization by detergent (Triton X 100). Adenosine Triphosphate 19-22 glucokinase Homo sapiens 132-143 33091480-9 2020 In addition, adenosine triphosphate (ATP)-activated currents in stellate ganglion neurons and HEK293 cells co-transfected with GCK and P2 x 3 receptor plasmids were reduced after GCK shRNA treatment. Adenosine Triphosphate 37-40 glucokinase Homo sapiens 127-130 33091480-9 2020 In addition, adenosine triphosphate (ATP)-activated currents in stellate ganglion neurons and HEK293 cells co-transfected with GCK and P2 x 3 receptor plasmids were reduced after GCK shRNA treatment. Adenosine Triphosphate 37-40 glucokinase Homo sapiens 179-182 32286938-1 2020 BACKGROUND: Glucokinase (GK), a cytoplasmic enzyme catalyzes the metabolism of glucose to glucose-6-phosphate with the help of ATP and aids in the controlling of blood glucose levels within normal range in humans. Adenosine Triphosphate 127-130 glucokinase Homo sapiens 12-23 32286938-1 2020 BACKGROUND: Glucokinase (GK), a cytoplasmic enzyme catalyzes the metabolism of glucose to glucose-6-phosphate with the help of ATP and aids in the controlling of blood glucose levels within normal range in humans. Adenosine Triphosphate 127-130 glucokinase Homo sapiens 25-27 31388064-0 2019 Identification of alkaline pH optimum of human glucokinase because of ATP-mediated bias correction in outcomes of enzyme assays. Adenosine Triphosphate 70-73 glucokinase Homo sapiens 47-58 31388064-7 2019 We demonstrated how the presence of ATP affects pH of widely used enzyme assay buffers and inversely affected KM of human hexokinase 2 and S0.5 of human glucokinase. Adenosine Triphosphate 36-39 glucokinase Homo sapiens 153-164 31388064-9 2019 We found that previously reported optimum of mammalian glucokinase was incorrect, affected by the ATP-induced pH shifts. Adenosine Triphosphate 98-101 glucokinase Homo sapiens 55-66 29885360-1 2018 Glucokinase (GK) is an enzyme that catalyzes the ATP-dependent phosphorylation of glucose to form glucose-6-phosphate, and it is a tightly regulated checkpoint in glucose homeostasis. Adenosine Triphosphate 49-52 glucokinase Homo sapiens 0-11 29885360-1 2018 Glucokinase (GK) is an enzyme that catalyzes the ATP-dependent phosphorylation of glucose to form glucose-6-phosphate, and it is a tightly regulated checkpoint in glucose homeostasis. Adenosine Triphosphate 49-52 glucokinase Homo sapiens 13-15 29648519-7 2018 The combined model (GK-GDH-core) shows that GK activity determines the energy state ([ATP]/[ADP][Pi]) in beta-cells for glucose concentrations > 5 mM ([ADP] < 35 microM). Adenosine Triphosphate 86-89 glucokinase Homo sapiens 20-22 29648519-7 2018 The combined model (GK-GDH-core) shows that GK activity determines the energy state ([ATP]/[ADP][Pi]) in beta-cells for glucose concentrations > 5 mM ([ADP] < 35 microM). Adenosine Triphosphate 86-89 glucokinase Homo sapiens 44-46