Literature summary for 3.1.5.1 extracted from

Singh, D.; Gawel, D.; Itsko, M.; Hochkoeppler, A.; Krahn, J.M.; London, R.E.; Schaaper, R.M.
Structure of Escherichia coli dGTP triphosphohydrolase a hexameric enzyme with DNA effector molecules (2015), J. Biol. Chem., 290, 10418-10429 .

Search for more literature for 3.1.5.1

Activating Compound

Activating Compound	Comment	Organism	Structure
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)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Protein Variants	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Escherichia coli	P15723	-	-

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Release 2023.1 (January 2023)