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3.6.1.23: dUTP diphosphatase

This is an abbreviated version!
For detailed information about dUTP diphosphatase, go to the full flat file.

Word Map on EC 3.6.1.23

Reaction

dUTP
+
H2O
=
dUMP
 +
diphosphate

Synonyms

DCD-DUT, dCTP deaminase-dUTPase, dCTP deaminase:dUTPase, deoxyuridine 5'-triphosphate, deoxyuridine 5'-triphosphate nucleotide hydrolase, deoxyuridine 5'-triphosphate nucleotidohydrolase, deoxyuridine 5'-triphosphate pyrophosphatase, deoxyuridine 50-triphosphate nucleotidohydrolase, deoxyuridine 5’-triphosphate nucleotidohydrolase, deoxyuridine nucleotidohydrolase, deoxyuridine triphosphatase, deoxyuridine triphosphate nucleotidohydrolase, deoxyuridine triphosphate pyrophosphatase, deoxyuridine-5'-triphosphate nucleotidohydrolase, deoxyuridine-triphosphate pyrophosphatase, desoxyuridine 5'-triphosphatase, desoxyuridine 5'-triphosphate nucleotidohydrolase, desoxyuridine-triphosphatase, DURP, DUT, DUT-N, DUT1, dUTP nucleotidohydrolase, dUTP pyrophosphatase, dUTPae, dUTPase, dUTPase-dUDPase, dUTPase-related protein, E165R, More, ORF 54, ORF8, P18, PIP4, Pr95, STSV2_30, Tb927.7.5160, U45, YncF, YosS

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.23 dUTP diphosphatase

Engineering

Engineering on EC 3.6.1.23 - dUTP diphosphatase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D33A
the enzyme activity of the mutant is almost totally abolished
D91A
the enzyme activity of the mutant is almost totally abolished
F154A
the mutant exhibits approximately 10.5% of the activity of the wild type enzyme
Q120A
the enzyme activity of the mutant is almost totally abolished
R71A
the mutant exhibits approximately 9.6% of the activity of the wild type enzyme
S72A
the mutant exhibits approximately 6.5% of the activity of the wild type enzyme
Y94A
the mutant exhibits approximately 10% of the activity of the wild type enzyme
D48E/N57S
-
active site mutant
E81S/T84R
DELTA160-187
-
truncated form
D81A
Dubowvirus dv80alpha
mutant presents a 3fold reduced dUTP-binding capacity and an extremely low hydrolytic activity. Mutant is unable to induce transcription of the Stl-repressed SaPIbov1 genes even when expressed at a high level
D81N
Dubowvirus dv80alpha
mutant presents a 3fold reduced dUTP-binding capacity and an extremely low hydrolytic activity
Y84A
Dubowvirus dv80alpha
mutation of a strictly conserved residue. Mutant shows a reduced dUTP-binding capacity but retains some enzymatic activity
Y84F
Dubowvirus dv80alpha
mutation of a strictly conserved residue, mutant presents almost wild-type dUTP-binding capacity and activity
Y84I
Dubowvirus dv80alpha
mutation of a strictly conserved residue. Complete loss of dUTP-binding capacity
Q93H
the mutant enzyme is significantly inhibited by staphylococcal repressor StlSaPIbov1 protein (Ki 0.00000483 mM)
Q93R
the mutant enzyme is significantly inhibited by staphylococcal repressor StlSaPIbov1 protein (Ki 0.0000059 mM)
R116S
-
the mutant shows 5.2% of wild type activity
S72A
site-directed mutagenesis, steady-state kinetic characterization, S72A mutation causes a 725fold reduction in kcat and a 35fold reduction in KM.
T22R/R116S
-
the mutant shows 2.5% of wild type activity
D49N/F158W
-
the Asp/Asn mutation within motif I results in approximately 1000fold decrease of steady-state rate and significantly weakens the interaction of the protein with alpha,beta-imido-dUTP (4fold) whereas dUMP binding is only slightly affected
F158A
-
the mutant shows severely decreased catalytic activity compared to the wild type enzyme
F158W
C4S
the mutant shows increased activity compared to the wild type enzyme
D131E
the mutant is completely devoid of enzymatic activity
D131N
the mutant shows decreased activity compared to the wild type enzyme
D131S
the mutant shows decreased activity compared to the wild type enzyme
D131S/G78D
the mutant shows decreased activity compared to the wild type enzyme
F273A
the deletion of the flexible C-terminal tail carrying motif V results in a protein completely devoid of enzymatic activity
R268A
the mutant shows decreased activity compared to the wild type enzyme
E145A
-
the mutant shows reduced specific activity towards dUTP
E145Q
-
the mutant shows reduced specific activity towards dUTP
D28N/H145W
the Asp/Asn mutation within Motif I results in approximately 50fold decrease of steady-state rate and significantly weakens the interaction of the protein with alpha,beta-imido-dUTP (15fold) whereas dUMP binding is only slightly affected
G143STOP
the mutant shows severely reduced activity compared to the wild type enzyme
H145A
the mutant shows decreased catalytic activity compared to the wild type enzyme
H145W
R40K/H145W
the mutant shows severely reduced activity compared to the wild type enzyme
T138STOP
the mutant shows severely reduced activity compared to the wild type enzyme
D28N/H145W
-
the Asp/Asn mutation within Motif I results in approximately 50fold decrease of steady-state rate and significantly weakens the interaction of the protein with alpha,beta-imido-dUTP (15fold) whereas dUMP binding is only slightly affected
-
G143STOP
-
the mutant shows severely reduced activity compared to the wild type enzyme
-
H145A
-
the mutant shows decreased catalytic activity compared to the wild type enzyme
-
H145W
R40K/H145W
-
the mutant shows severely reduced activity compared to the wild type enzyme
-
T138STOP
-
the mutant shows severely reduced activity compared to the wild type enzyme
-
F46A
the mutation does not affect the nucleotide hydrolase activity of dUTPase
I117A
the mutation does not affect the nucleotide hydrolase activity of dUTPase
K96A
the mutation does not affect the nucleotide hydrolase activity of dUTPase
D32A
the mutant exhibits negligible activity
D85A
the mutant exhibits negligible activity
D87A
the mutant exhibits negligible activity
D87A/R137A/D85A
inactive
F142A
the mutant exhibits very low activity
G82S
allele dut1-1 of gene dut1 possesses a single amino acid substitution in a conserved motif nearby the active site and exhibits a greatly reduced dUTPase activity, dut1-1 single mutant exhibits growth delay and cell cycle abnormalities and shows a strong spontaneous mutator phenotype, the dut1-1 allele is deleterious in wild-type strain and AP sites repair defective mutants, overview. The dut1-1 mutant is a spontaneous mutator that accumulates AT to CG transversions
Q114A
the mutant shows essentially the wild type affinity for dUTP and greatly reduced activity
R111A
the mutant has reduced activity and lower substrate affinity (increased Km) compared to the wild type enzyme
R137A
the mutant exhibits negligible activity
R68A
the mutant exhibits very low activity
S69A
the mutant exhibits negligible activity
Y88A
the mutant protein is equally active against both dUTP and UTP and has reduced activity and lower substrate affinity (increased Km) compared to the wild type enzyme
D170G
the mutant shows 68% of wild type activity
D170L
the mutant shows 1.7% of wild type activity
D34N
the mutant shows 1.6% of wild type activity
DELTA134-153
the mutant shows 0.73% of wild type activity
DELTA161-170
inactive
DELTA170-171
the mutant shows 14% of wild type activity
F166Y
the mutant shows 5.5% of wild type activity
K150A
the mutant shows 54% of wild type activity
K150E
the mutant shows 49% of wild type activity
R158A
the mutant shows 28% of wild type activity
R158E
the mutant shows 23% of wild type activity
R158W
the mutant shows 22% of wild type activity
R161K
the mutant shows 0.23% of wild type activity
R24T
the mutant shows 3.6% of wild type activity
R24T/S115R
the mutant shows 1.8% of wild type activity
R24T/S115R/D170G
the mutant shows 17% of wild type activity
S115R
the mutant shows 13% of wild type activity
V160D
the mutant shows 85% of wild type activity
additional information