dUTP diphosphatase

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In enzymology, a dUTP diphosphatase (EC 3.6.1.23) is an enzyme that catalyzes the chemical reaction

dUTP + H₂O $\rightleftharpoons$ dUMP + diphosphate

Thus, the two substrates of this enzyme are dUTP and H₂O, whereas its two products are dUMP and diphosphate.

This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is dUTP nucleotidohydrolase. Other names in common use include deoxyuridine-triphosphatase, dUTPase, dUTP pyrophosphatase, desoxyuridine 5'-triphosphate nucleotidohydrolase, and desoxyuridine 5'-triphosphatase. This enzyme participates in pyrimidine metabolism.

The main function of this enzyme is to remove dUTP from the deoxynucleotide pool, which reduces the probability of this base being mistakenly incorporated into DNA by DNA polymerases, which is a cause of mutations.^[1]

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 48 structures have been solved for this class of enzymes, with PDB accession codes 1DUC, 1DUD, 1DUN, 1DUP, 1DUT, 1EU5, 1EUW, 1F7D, 1F7K, 1F7N, 1F7O, 1F7P, 1F7Q, 1F7R, 1MQ7, 1OGH, 1OGK, 1OGL, 1PKH, 1PKJ, 1PKK, 1RN8, 1RNJ, 1SEH, 1SIX, 1SJN, 1SLH, 1SM8, 1SMC, 1SNF, 1SYL, 1VYQ, 1W2Y, 2BSY, 2BT1, 2CJE, 2D4L, 2D4M, 2D4N, 2HQU, 2HR6, 2HRM, 2OKB, 2OKD, 2OKE, 2OL0, 2OL1, and 2PY4.

[edit] References

^ Vassylyev DG, Morikawa K (1996). "Precluding uracil from DNA". Structure 4 (12): 1381–5. doi:10.1016/S0969-2126(96)00145-1. PMID 8994964.

IUBMB entry for 3.6.1.23
BRENDA references for 3.6.1.23 (Recommended.)
PubMed references for 3.6.1.23
PubMed Central references for 3.6.1.23
Google Scholar references for 3.6.1.23
Bertani Le., Haeggmark A., Reichard P. (1963). "Enzymatic Synethesis of Deoxyribonucleotides. II. Formation and Interconversion of Deoxyuridine Phosphates". J. Biol. Chem. 238: 3407–13. PMID 14085395.
Giroir LE, Deutsch WA (1987). "Drosophila deoxyuridine triphosphatase. Purification and characterization". J. Biol. Chem. 262: 130–4. PMID 3025197.
Greenberg Gr., Somerville Rl. (1962). "Deoxyuridylate kinase activity and deoxyuridinetriphosphatase in Escherichia coli". Proc. Natl. Acad. Sci. U. S. A. 48: 247–57. doi:10.1073/pnas.48.2.247. PMID 13901467.
Grindey GR, Nichol CA (1971). "Mammalian deoxyuridine 5'-triphosphate pyrophosphatase". Biochim. Biophys. Acta. 240: 180–3. PMID 5105331.