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3.6.1.56: 2-hydroxy-dATP diphosphatase

This is an abbreviated version!
For detailed information about 2-hydroxy-dATP diphosphatase, go to the full flat file.

Word Map on EC 3.6.1.56

Reaction

2-hydroxy-dATP
+
H2O
=
2-hydroxy-dAMP
 +
diphosphate

Synonyms

(2'-deoxy) ribonucleoside 5'-triphosphate pyrophosphohydrolase, 8-oxo-dGTP hydrolase, hMTH1, MTH1, MTH2, MutT homologue 1, Nud2, Nudix hydrolase 2, NUDT1

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.56 2-hydroxy-dATP diphosphatase

Engineering

Engineering on EC 3.6.1.56 - 2-hydroxy-dATP diphosphatase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D119A
D119N
D120A
-
the mutant shows 8% of wild type activity
D120N
-
the mutant shows 4% of wild type activity
L150A
mutant enzyme with decrased thermostability. Tm-value is 50°C compared to 65°C for the wild-type enzyme
M116L
the mutation causes a considerable drop in activity with dGTP compared to the wild type enzyme
N33A
mutation decreases catalytic activity toward 2-hydroxy-dATP to 5% of the wild-type activity. The mutant shows 14% of the wild-type 8-oxo-dGTP activity
N33E
mutation decreases catalytic activity toward 2-hydroxy-dATP to 53% of the wild-type activity. Activity towards 8-oxo-dGTP is totally abolished
V156A
mutant enzyme with decrased thermostability. Tm-value is 61°C compared to 65°C for the wild-type enzyme
V83M
-
Met83-MTH1 is more thermolabile than that of Val83-MTH1. Substitution of valine for methionine at the residue 83 of MTH1 protein appears to lead to alteration in the secondary structure which renders the protein more labile than the normal type protein
W117A
W117Y
L116M
the mutation causes a considerable drop in activity with dGTP compared to the wild type enzyme
A84G
-
the mutant shows about 70% of wild type activity
A84G/G90E
-
the mutant shows about 110% of wild type activity
G90E
-
the mutant shows about 130% of wild type activity
additional information
sequence comparison with the Escherichia coli homolog, MutT, which hydrolyzes only 8-oxo-dGTP and 8-oxo-GTP but not oxidized forms of dATP or ATP. Neither a replacement of the phosphohydrolase module of MTH1 with that of MutT nor deletions of the C-terminal region of MTH1, which is unique for MTH1, alter the substrate specificity of MTH1. In contrast, the substitution of residues at position Trp117 and Asp119 of MTH1, which show apparent chemical shift perturbations with 8-oxo-dGDP in NMR analyses but are not conserved in MutT, affected the substrate specificity. Trp117 is essential for MTH1 to recognize both 8-oxo-dGTP and 2-hydroxy-dATP, whereas Asp119 is only essential for recognizing 2-hydroxy-dATP, thus suggesting that origins of the substrate-binding pockets for MTH1 and MutT are different