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Literature summary extracted from
- Structure of Escherichia coli dGTP triphosphohydrolase a hexameric enzyme with DNA effector molecules (2015), J. Biol. Chem., 290, 10418-10429 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.5.1 | single-stranded DNA | Dgt preparations lacking DNA are able to bind single-stranded DNA with high affinity. DNA binding positively affects the activity of the enzyme. dGTPase activity displays sigmoidal (cooperative) behavior without DNA but hyperbolic (Michaelis-Menten) kinetics in its presence, consistent with a specific lowering of the apparent Km for dGTP | Escherichia coli |  |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.5.1 | expression in Escherichia coli | Escherichia coli |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.1.5.1 | structure at 3.1 A resolution. The protein hexamer contains two molecules of single-stranded DNA, causing significant conformational changes in the enzyme, including in the catalytic site of the enzyme | Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.5.1 | S34D/G37E | residue changes in the DNA binding cleft. The mutant enzyme is still active, but incapable of DNA binding and cannot be stimulated by addition of DNA | Escherichia coli |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.5.1 | Escherichia coli | P15723 | - |
- |
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Release 2023.1 (January 2023)
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