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3.1.5.B1: dNTPase

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

Word Map on EC 3.1.5.B1

Reaction

dNTP
+
H2O
=
a deoxynucleotide
 +
Triphosphate

Synonyms

deoxynucleoside triphosphate triphosphohydrolase, deoxyribonucleotide triphosphohydrolase, EF_1143, HD domain protein, SAMHD1

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.5 Triphosphoric-monoester hydrolases
                3.1.5.B1 dNTPase

Crystallization

Crystallization on EC 3.1.5.B1 - dNTPase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure in complex with dGTP and dTTP, to 2.35 A resolution. The tetrameric enzyme EF1143 contains four additional secondary allosteric sites adjacent to the previously identified dGTP-binding primary regulatory sites. dGTP binding to the first allosteric site, with nanomolar affinity, is a prerequisite for substrate docking and hydrolysis. Then, the presence of a particular dNTP in the second site either enhances or inhibits the dNTPase activity
in complex with the allosteric activator and substrate dGTP/dATP, to 1.8 A resolution
-
structures of the catalytic core of SAMHD1 in complex with different combinations of GTP and dNTPs. SAMHD1 contains two activator-binding sites in the allosteric pocket. The primary activator GTP binds to one site and the substrate dNTP (dATP, dCTP, dUTP or dTTP) occupies the other. Both GTP and dNTP are required for tetramer activation of the enzyme. In the absence of substrate binding, SAMHD1 adopts an inactive dimer conformation even when complexed with GTP
structures of variants T592E and T592V. Mutation T592E induces large conformational changes, likely triggered by electrostatic repulsion from a distinct negatively charged environment surrounding residue Thr-592