Literature summary for 3.1.5.B1 extracted from

Vorontsov, I.I.; Wu, Y.; DeLucia, M.; Minasov, G.; Mehrens, J.; Shuvalova, L.; Anderson, W.F.; Ahn, J.
Mechanisms of allosteric activation and inhibition of the deoxyribonucleoside triphosphate triphosphohydrolase from Enterococcus faecalis (2014), J. Biol. Chem., 289, 2815-2824.

Activating Compound

Activating Compound	Comment	Organism
dATP	both dATP and dGTP are co-activators for hydrolysis of dTTP, dATP might bind at the secondary allosteric site	Enterococcus faecalis
dCTP	allosteric activator, less potent than dGTP and dATP	Enterococcus faecalis
dGTP	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	Enterococcus faecalis

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Enterococcus faecalis

Crystallization (Comment)

Organism

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

Enterococcus faecalis

Protein Variants

Protein Variants	Comment	Organism
H114A	no residual activity	Enterococcus faecalis
H129A	less than 5% residual activity	Enterococcus faecalis
K14A	less than 5% residual activity	Enterococcus faecalis
K330A	no residual activity	Enterococcus faecalis
N36A	no residual activity	Enterococcus faecalis
Q241A	about 10% residual activity	Enterococcus faecalis
Q41A	less than 5% residual activity	Enterococcus faecalis
R17A	no residual activity	Enterococcus faecalis
R17Q	about 5% residual activity	Enterococcus faecalis
R206A/R209A	no residual activity	Enterococcus faecalis
R206Q	about 30% residual activity	Enterococcus faecalis
R209S	about 70% residual activity	Enterococcus faecalis
R326A	about 40% residual activity	Enterococcus faecalis
Y199A	no residual activity	Enterococcus faecalis

Organism

Organism	UniProt	Comment	Textmining
Enterococcus faecalis	Q836G9	-	-
Enterococcus faecalis ATCC 700802	Q836G9	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	enzyme EF1143 fails to hydrolyze any of the dNTPs when a sole dNTP is present in the reaction mixture. Among the four dNTPs, only dGTP can function as an activator of dATP and dCTP hydrolysis. dGTP hydrolysis is clearly enhanced by the presence of dATP or dCTP, but not dTTP, with dATP being the more potent activator. Further, dTTP hydrolysis is virtually nonexistent when any one other dNTP is combined with dTTP in the reaction mixture. With all four dNTPs present at equal concentrations, the decreasing order of dNTP hydrolysis is dGTP, dCTP, dATP, dTTP	Enterococcus faecalis	?	-	?
additional information	enzyme EF1143 fails to hydrolyze any of the dNTPs when a sole dNTP is present in the reaction mixture. Among the four dNTPs, only dGTP can function as an activator of dATP and dCTP hydrolysis. dGTP hydrolysis is clearly enhanced by the presence of dATP or dCTP, but not dTTP, with dATP being the more potent activator. Further, dTTP hydrolysis is virtually nonexistent when any one other dNTP is combined with dTTP in the reaction mixture. With all four dNTPs present at equal concentrations, the decreasing order of dNTP hydrolysis is dGTP, dCTP, dATP, dTTP	Enterococcus faecalis ATCC 700802	?	-	?

Synonyms

Synonyms	Comment	Organism
EF_1143	-	Enterococcus faecalis
HD domain protein	-	Enterococcus faecalis