Ketohexokinase
From Proteopedia
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<StructureSection load='3q92' size='350' side='right' caption='Human ketohexokinase complex with ihibitor and sulfate (PDB entry [[3q92]])' scene='48/484861/Cv/1'> | <StructureSection load='3q92' size='350' side='right' caption='Human ketohexokinase complex with ihibitor and sulfate (PDB entry [[3q92]])' scene='48/484861/Cv/1'> | ||
== Function == | == Function == | ||
| - | '''Ketohexokinase''' (KHK) also known as hepatic fructokinase catalyzes the phosphorylation of fructose to fructose-1-phosphate using ATP as phosphate source in the liver. The HKH gene is spliced to HKH-A and the more active HKH-C. KHK acts in the first step of fructose metabolism<ref>PMID:2996495</ref>. | + | '''Ketohexokinase''' (KHK) also known as '''hepatic fructokinase''' catalyzes the phosphorylation of fructose to fructose-1-phosphate using ATP as phosphate source in the liver. The HKH gene is spliced to HKH-A and the more active HKH-C. KHK acts in the first step of fructose metabolism<ref>PMID:2996495</ref>. |
== Disease == | == Disease == | ||
Revision as of 09:44, 3 July 2019
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3D structures of ketohexokinase
2hlz, 2hqq, 3b3l – hKHK – human
2hw1, 3nbv – hKHK + AMPPNP + fructose
3nbw – hKHK + pyrazole derivative
3nc2, 3nc9, 3nca, 3ro4, 3q92, 3qa2, 3qai, 5wbm, 5wbo, 5wbp, 5wbq, 5wbr, 5wbz – hKHK + inhibitor
References
- ↑ Bais R, James HM, Rofe AM, Conyers RA. The purification and properties of human liver ketohexokinase. A role for ketohexokinase and fructose-bisphosphate aldolase in the metabolic production of oxalate from xylitol. Biochem J. 1985 Aug 15;230(1):53-60. PMID:2996495
- ↑ Asipu A, Hayward BE, O'Reilly J, Bonthron DT. Properties of normal and mutant recombinant human ketohexokinases and implications for the pathogenesis of essential fructosuria. Diabetes. 2003 Sep;52(9):2426-32. PMID:12941785
- ↑ Maryanoff BE, O'Neill JC, McComsey DF, Yabut SC, Luci DK, Jordan AD Jr, Masucci JA, Jones WJ, Abad MC, Gibbs AC, Petrounia I. Inhibitors of Ketohexokinase: Discovery of Pyrimidinopyrimidines with Specific Substitution that Complements the ATP-Binding Site. ACS Med Chem Lett. 2011 Apr 18;2(7):538-43. doi: 10.1021/ml200070g. eCollection, 2011 Jul 14. PMID:24900346 doi:http://dx.doi.org/10.1021/ml200070g
