Uridylate kinase
From Proteopedia
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| - | <StructureSection load='2j4k' size=' | + | <StructureSection load='2j4k' size='400' side='right' caption='Uridylate kinase hexamer complex with ligand UMP (stick model), Cd+ (gold) and Mg+2 (green) ions [[2j4k]]' scene='48/487531/Cv/1' > |
== Function == | == Function == | ||
'''Uridylate kinase''' (UK) catalyzes the reversible transfer of phosphate from UMP to UDP using ATP as a phosphate source. UDP is the starting point of synthesis of all other pyrimidine nucleotides. The eukaryotic UK has specificity to both UMP and CMP while the bacterial one is specific for UMP. The bacterial UK is Mg+2 dependent and is activated by GTP and repressed by UTP. The bacterial UK is composed of a C terminal ATP-binding domain and an N terminal UMP-binding domain<ref>PMID:10218107</ref>. | '''Uridylate kinase''' (UK) catalyzes the reversible transfer of phosphate from UMP to UDP using ATP as a phosphate source. UDP is the starting point of synthesis of all other pyrimidine nucleotides. The eukaryotic UK has specificity to both UMP and CMP while the bacterial one is specific for UMP. The bacterial UK is Mg+2 dependent and is activated by GTP and repressed by UTP. The bacterial UK is composed of a C terminal ATP-binding domain and an N terminal UMP-binding domain<ref>PMID:10218107</ref>. | ||
Revision as of 08:28, 14 December 2016
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3D structures of uridylate kinase
Updated on 14-December-2016
References
- ↑ Yan H, Tsai MD. Nucleoside monophosphate kinases: structure, mechanism, and substrate specificity. Adv Enzymol Relat Areas Mol Biol. 1999;73:103-34, x. PMID:10218107
- ↑ Jensen KS, Johansson E, Jensen KF. Structural and enzymatic investigation of the Sulfolobus solfataricus uridylate kinase shows competitive UTP inhibition and the lack of GTP stimulation. Biochemistry. 2007 Mar 13;46(10):2745-57. Epub 2007 Feb 13. PMID:17297917 doi:10.1021/bi0618159
