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Information on EC 3.6.1.23 - dUTP diphosphatase and Organism(s) Mason-Pfizer monkey virus and UniProt Accession P07570

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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.23 dUTP diphosphatase
IUBMB 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.
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This record set is specific for:
Mason-Pfizer monkey virus
UNIPROT: P07570
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The taxonomic range for the selected organisms is: Mason-Pfizer monkey virus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
dUTP
+
H2O
=
dUMP
+
diphosphate
+
=
+
Synonyms
dutpase, deoxyuridine triphosphatase, deoxyuridine triphosphate nucleotidohydrolase, deoxyuridine 5'-triphosphate nucleotidohydrolase, dut-n, deoxyuridine 5'-triphosphate, dutp pyrophosphatase, dutp nucleotidohydrolase, orf 54, dcd-dut, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deoxyuridine 5'-triphosphate nucleotidohydrolase
-
-
desoxyuridine 5'-triphosphatase
-
-
-
-
desoxyuridine 5'-triphosphate nucleotidohydrolase
-
-
-
-
desoxyuridine-triphosphatase
-
-
-
-
dUTP pyrophosphatase
-
-
-
-
dUTPase
P18
-
-
-
-
PIP4
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
dUTP nucleotidohydrolase
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.
CAS REGISTRY NUMBER
COMMENTARY hide
37289-34-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha,beta-imido-dUTP + H2O
dUMP + amino-diphosphate
show the reaction diagram
O92810
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PRO_MPMV
911
0
100648
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
-
homotrimer, crystal structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with nucleotides. Reaction starts with dUTPase capturing and properly positioning two substrates: dUTP and the catalytic water molecule. the catalytic water molecule is placed near the alpha-phosphate group opposite from the leaving group. Hydrolysis is then initiated by nucleophilic attack of Wthe water on the alpha-phosphate along the line of the scissile bond (in-line attack). A symmetric phosphorane-like transition state structure is formed with significant bond order in both forming and breaking bonds. Bond breaking is concomitant with inversion of the alpha-phosphate configuration and diphosphate-Mg2+ escape. The dUMP product then relaxes by rotation of the alpha-phosphate group and establishes a configuration similar to the one observed for this moiety in the E-S complex
O92810
purified recombinant C-terminal domain nucleocapsid fusion enzyme, hanging drop vapour diffusion method, 5 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 0.2 M NH4Cl, 10 mM MgCl2, 5 mM DTT, and 0.5 mM PMSF, with or without 1.3 mM alpha,beta-imino-dUTP, room temperature, mixed 1:1 with reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 8% w/v PEG 8000, X-ray diffraction structure determination and analysis at 1.75-2.3 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminal domain nucleocapsid fusion protein or free enzyme from Escherichia coli by heparin affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression as C-terminal domain fusion protein with the nucleocapsid protein in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Barabas, O.; Nemeth, V.; Vertessy, B.G.
Crystallization and preliminary X-ray studies of dUTPase from Mason-Pfizer monkey retrovirus
Acta Crystallogr. Sect. F
F62
399-401
2006
Mason-Pfizer monkey virus
Manually annotated by BRENDA team
Barabas, O.; Nemeth, V.; Bodor, A.; Perczel, A.; Rosta, E.; Kele, Z.; Zagyva, I.; Szabadka, Z.; Grolmusz, V.I.; Wilmanns, M.; Vertessy, B.G.
Catalytic mechanism of ?-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling
Nucleic Acids Res.
41
10542-10555
2013
Mason-Pfizer monkey virus (O92810)
Manually annotated by BRENDA team
Hizi, A.; Herzig, E.
dUTPase the frequently overlooked enzyme encoded by many retroviruses
Retrovirology
12
70
2015
bovine immunodeficiency virus, Caenorhabditis elegans, Caprine arthritis encephalitis virus, equine infectious anemia virus, Escherichia coli (P06968), feline immunodeficiency virus, Homo sapiens (P33316), Homo sapiens, Human endogenous retrovirus K, Human gammaherpesvirus 4, Human gammaherpesvirus 8, Jembrana disease virus, Mason-Pfizer monkey virus, mouse mammary tumor virus, Murid gammaherpesvirus 4, Mycobacterium tuberculosis, Plasmodium falciparum, Saccharomyces cerevisiae, Visna-maedi virus
Manually annotated by BRENDA team