Uridylate kinase

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^[1].

Structural highlights

The biological assembly of Uridylate kinase from Sulfolobus solfataricus (2j4k) is . The and excludes purine nucleotides^[2]. Water molecule is shown as red sphere.

Uridylate kinase hexamer complex with ligand UMP, Cd+ (gold) and Mg+2 (green) ions 2j4k

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3D structures of uridylate kinase3D structures of uridylate kinase

Updated on 21-June-2022

ReferencesReferences

↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

[1] 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

[2] 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

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