EC Number   |
Application |
Reference |
|---|
   2.7.1.3 | analysis |
development of a three-dimensional chemical-feature-based QSAR pharmacophore model by using Discovery Studio v2.5 to identify inhibitors, and screening of chemical databases for validated pharmacophore hypothesis. Hit compounds show good hydrogen bonding interactions with the keyamino acids such as Arg108, Asp258, Gly41, Gly255, Asn42 and water molecules W12, W27, respectively |
737891 |
| 2.7.1.3 | medicine |
compared with normal hepatocytes, hepatocellular carcinoma cells markedly reduce the rate of fructose metabolism and the level of reactive oxygen species, as a result of a c-Myc-dependent and heterogeneous nuclear ribonucleoprotein H1- and H2-mediated switch from expression of the high-activity fructokinase KHK-C to the low-activity KHK-A isoform. KHK-A acts as a protein kinase, phosphorylating and activating phosphoribosyl pyrophosphate synthetase PRPS1. c-Myc, hnRNPH1/2 and KHK-A expression levels and PRPS1 Thr225 phosphorylation levels correlate with each other in hepatocellular carcinoma specimens and are associated with poor prognosis for hepatocellular carcinoma |
739133 |
| 2.7.1.3 | medicine |
mutually exclusive splicing of adjacent exons 3A and 3C in ketohexokinase precursor RNA results in expression of ketohexokinase isoform KHK-A or KHK-C. KHK-A but not KHK-C interacts with phosphoribosyl diphosphate synthetase PRPS1. KHK-A functions as a protein kinase and directly phosphorylates PRPS1 at T225. This phosphorylation blocks the binding of the allosteric inhibitor ADP to PRPS1, thereby abrogating the feedback inhibition by ADP and leading to elevated de novo nucleic acid synthesis by constitutively activating PRPS1 in hepytocellular carcinoma cells |
737995 |
