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Information on EC 3.6.1.23 - dUTP diphosphatase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9STG6
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3.6.1.23 dUTP diphosphataseIUBMB 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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Word Map
- 3.6.1.23
- uracil
- dump
- trimer
- thymidylate
-
misincorporation
- glycosylase
-
herpes
-
uracil-dna
- simplex
- drug development
-
homotrimeric
- herpesviruses
-
integrase
-
fluoropyrimidines
-
uracil-containing
- lentiviruses
- pyrophosphatases
-
sapis
-
ebv-encoded
- herv-k
- 2'-deoxyuridine
-
varicella-zoster
- fiv
- diagnostics
- medicine
- pharmacology
- synthesis
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
dutpase, deoxyuridine triphosphatase, deoxyuridine triphosphate nucleotidohydrolase, deoxyuridine 5'-triphosphate nucleotidohydrolase, dut-n, deoxyuridine 5'-triphosphate, dutp pyrophosphatase, dutp nucleotidohydrolase, orf 54, dcd-dut, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
desoxyuridine 5'-triphosphatase
-
-
-
-
desoxyuridine 5'-triphosphate nucleotidohydrolase
-
-
-
-
desoxyuridine-triphosphatase
-
-
-
-
dUTP pyrophosphatase
-
-
-
-
dUTPase
-
-
-
-
P18
-
-
-
-
PIP4
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -
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
37289-34-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dUTP + H2O
dUMP + diphosphate
the enzyme is responsible for maintaining a low dUTP level in order to avoid the incorporation of uracil into DNA, and for providing dUMP as a substrate for deoxythymidine triphosphate biosynthesis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dUTP + H2O
dUMP + diphosphate
the enzyme is responsible for maintaining a low dUTP level in order to avoid the incorporation of uracil into DNA, and for providing dUMP as a substrate for deoxythymidine triphosphate biosynthesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DUT_ARATH
166
0
17557
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 50 mM Tris-HCl at pH 7.4 and 5 mM of the non-hydrolyzable ligand analog 2'-deoxyuridine 5'-[(alpha,beta)-imido]-triphosphate
purified recombinant enzyme, hanging drop vapour diffusion method, 25°C, 0.001 ml of protein solution containing 10 mg/ml protein in 50 mM Tris-HCl, pH 7.4, is mixed with 0.001 ml of reservoir solution containing 2 M ammonium sulfate and 0.1 M Tris-HCl, pH 8.5, X-ray diffraction structure determination and analysis at 2.2-2.3 A resolution, molecular replacement
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bajaj, M.; Moriyama, H.
Purification, crystallization and preliminary crystallographic analysis of deoxyuridine triphosphate nucleotidohydrolase from Arabidopsis thaliana
Acta Crystallogr. Sect. F
63
409-411
2007
Arabidopsis thaliana (Q9STG6), Arabidopsis thaliana
Inoguchi, N.; Chaiseeda, K.; Yamanishi, M.; Kim, M.K.; Jang, Y.; Bajaj, M.; Chia, C.P.; Becker, D.F.; Moriyama, H.
Structural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase the role of tryptophan 93 in ligand orientation
BMC Res. Notes
8
784
2015
Arabidopsis thaliana (Q9STG6), Arabidopsis thaliana
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