DUTP diphosphatase

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

There are at least two structurally distinct families of dUTPases. The crystal structure of human dUTPase reveals that each subunit of the dUTPase trimer folds into an eight-stranded jelly-roll beta barrel, with the C-terminal beta strands interchanged among the subunits. The structure is similar to that of the Escherichia coli enzyme, despite low sequence homology between the two enzymes.{{cite journal | vauthors = Mol CD, Harris JM, McIntosh EM, Tainer JA | title = Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits | journal = Structure | volume = 4 | issue = 9 | pages = 1077–92 |date=September 1996 | pmid = 8805593 | doi = 10.1016/S0969-2126(96)00114-1| doi-access = free }}

The second family has a novel all-alpha fold, members of this family are unrelated to the all-beta fold found in dUTPases of the majority of organisms.{{Cite journal

| last1 = Moroz | first1 = O. V.

| last2 = Harkiolaki | first2 = M.

| last3 = Galperin | first3 = M. Y.

| last4 = Vagin | first4 = A. A.

| last5 = González-Pacanowska | first5 = D.

| last6 = Wilson | first6 = K. S.

| doi = 10.1016/j.jmb.2004.07.050

| title = The Crystal Structure of a Complex of Campylobacter jejuni dUTPase with Substrate Analogue Sheds Light on the Mechanism and Suggests the "Basic Module" for Dimeric d(C/U)TPases

| journal = Journal of Molecular Biology

| volume = 342

| issue = 5

| pages = 1583–1597

| year = 2004

| pmid = 15364583

}}

• DUT, the gene that codes for this enzyme in humans
• DnaS or dut, the gene that codes for this enzyme in E. coli

{{reflist|1}}

• {{cite journal |author1 = Bertani Le. |author2 =Haeggmark A. |author3 =Reichard P.| year = 1963 | title = Enzymatic Synthesis of Deoxyribonucleotides. II. Formation |author4 =Interconversion of Deoxyuridine Phosphates | journal = J. Biol. Chem. | volume = 238 |issue =10 | pages = 3407–13 |doi =10.1016/S0021-9258(18)48681-4 | pmid = 14085395 |doi-access =free }}
• {{cite journal | vauthors = Giroir LE, Deutsch WA | year = 1987 | title = Drosophila deoxyuridine triphosphatase. Purification and characterization | journal = J. Biol. Chem. | volume = 262 | pages = 130–4 | pmid = 3025197 | issue = 1 | doi = 10.1016/S0021-9258(19)75898-0 | doi-access = free }}
• {{cite journal | vauthors = Greenberg G, Somerville R | title = Deoxyuridylate Kinase Activity and Deoxyuridinetriphosphatase in Escherichia Coli | year = 1962 | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 48 | pages = 247–57 | pmid = 13901467 | doi = 10.1073/pnas.48.2.247 | pmc = 220766 | issue = 2 | bibcode = 1962PNAS...48..247G | doi-access = free }}
• {{cite journal |vauthors=Grindey GR, Nichol CA | year = 1971 | title = Mammalian deoxyuridine 5'-triphosphate pyrophosphatase | journal = Biochim. Biophys. Acta | volume = 240 | pages = 180–3 | pmid = 5105331 | issue = 2 | doi=10.1016/0005-2787(71)90655-1}}

{{InterPro content|IPR008180}}

{{InterPro content|IPR014871}}

{{Acid anhydride hydrolases}}

{{Enzymes}}

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Category:EC 3.6.1

Category:Enzymes of known structure

{{3.6-enzyme-stub}}