ExplorEnz: EC 3.6.1.23

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3.6.1.23

Accepted name:

dUTP diphosphatase

Reaction:

dUTP + H₂O = dUMP + diphosphate

Other name(s):

DUT (gene name); deoxyuridine-triphosphatase; dUTPase; dUTP pyrophosphatase; desoxyuridine 5′-triphosphate nucleotidohydrolase; desoxyuridine 5′-triphosphatase

Systematic name:

dUTP nucleotidohydrolase

Comments:

The enzyme catalyses the Mg²⁺-dependent hydrolysis of dUTP to dUMP, providing the substrate for EC 2.1.1.45, thymidylate synthase, leading to production of thymidine nucleotides. By reducing the effective ratio of dUTP to TTP, the enzyme also reduces the possibility of dUTP incorporation into DNA.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37289-34-2

References:

1.	Greenberg, G.R. and Somerville, R.L. Deoxyuridylate kinase activity and deoxyuridinetriphosphatase in Escherichia coli. Proc. Natl. Acad. Sci. USA 48 (1962) 247–257. [PMID: 13901467]
2.	Bertani, L.E., Häggmark, A. and Reichard, P. Enzymatic synthesis of deoxyribonucleotides. II. Formation and interconversion of deoxyuridine phosphates. J. Biol. Chem. 238 (1963) 3407–3413. [PMID: 14085395]
3.	Grindey, G.B. and Nichol, C.A. Mammalian deoxyuridine 5′-triphosphate pyrophosphatase. Biochim. Biophys. Acta 240 (1971) 180–183. [DOI] [PMID: 5105331]
4.	Shlomai, J. and Kornberg, A. Deoxyuridine triphosphatase of Escherichia coli. Purification, properties, and use as a reagent to reduce uracil incorporation into DNA. J. Biol. Chem. 253 (1978) 3305–3312. [PMID: 346589]
5.	Giroir, L.E. and Deutsch, W.A. Drosophila deoxyuridine triphosphatase. Purification and characterization. J. Biol. Chem. 262 (1987) 130–134. [PMID: 3025197]
6.	Cedergren-Zeppezauer, E.S., Larsson, G., Nyman, P.O., Dauter, Z. and Wilson, K.S. Crystal structure of a dUTPase. Nature 355 (1992) 740–743. [DOI] [PMID: 1311056]
7.	Ladner, R.D., McNulty, D.E., Carr, S.A., Roberts, G.D. and Caradonna, S.J. Characterization of distinct nuclear and mitochondrial forms of human deoxyuridine triphosphate nucleotidohydrolase. J. Biol. Chem. 271 (1996) 7745–7751. [DOI] [PMID: 8631816]
8.	Bajaj, M. and Moriyama, H. Purification, crystallization and preliminary crystallographic analysis of deoxyuridine triphosphate nucleotidohydrolase from Arabidopsis thaliana. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 (2007) 409–411. [DOI] [PMID: 17565183]
9.	Varga, B., Barabas, O., Kovari, J., Toth, J., Hunyadi-Gulyas, E., Klement, E., Medzihradszky, K.F., Tolgyesi, F., Fidy, J. and Vertessy, B.G. Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase. FEBS Lett. 581 (2007) 4783–4788. [DOI] [PMID: 17880943]

[EC 3.6.1.23 created 1972]