Literature summary for 2.7.1.147 extracted from

Merino, F.; Rivas-Pardo, J.A.; Caniuguir, A.; Garcia, I.; Guixe, V.
Catalytic and regulatory roles of divalent metal cations on the phosphoryl-transfer mechanism of ADP-dependent sugar kinases from hyperthermophilic archaea (2012), Biochimie, 94, 516-524.

Search for more literature for 2.7.1.147

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Pyrococcus furiosus
expressed in Escherichia coli	Pyrococcus horikoshii
expressed in Escherichia coli	Thermococcus litoralis

Inhibitors

Inhibitors	Comment	Organism	Structure
ADP	-	Pyrococcus furiosus
ADP	-	Pyrococcus horikoshii
ADP	-	Thermococcus litoralis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.008	-	ADP	in the presence of 1 mM Mg2+, pH 6.5, 50°C	Pyrococcus horikoshii
0.008	-	ADP	in the presence of 1 mM Mn2+, pH 6.5, 50°C	Pyrococcus horikoshii
0.014	-	ADP	in the presence of 1 mM Mg2+, pH 7.8, 40°C	Pyrococcus furiosus
0.015	-	ADP	in the presence of 1 mM Co2+, pH 7.8, 40°C	Thermococcus litoralis
0.017	-	ADP	in the presence of 1 mM Mn2+, pH 7.8, 40°C	Thermococcus litoralis
0.022	-	ADP	in the presence of 1 mM Co2+, pH 6.5, 50°C	Pyrococcus horikoshii
0.022	-	ADP	in the presence of 1 mM Mn2+, pH 7.8, 40°C	Pyrococcus furiosus
0.023	-	ADP	in the presence of 1 mM Mg2+, pH 7.8, 40°C	Thermococcus litoralis
0.025	-	ADP	in the presence of 1 mM Co2+, pH 7.8, 40°C	Pyrococcus furiosus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	-	Pyrococcus furiosus
Co2+	-	Pyrococcus horikoshii
Co2+	highest kcat/Km value obtained	Thermococcus litoralis
Mg2+	-	Thermococcus litoralis
Mg2+	highest kcat/Km value obtained	Pyrococcus furiosus
Mg2+	highest kcat/Km value obtained	Pyrococcus horikoshii
Mn2+	-	Pyrococcus furiosus
Mn2+	-	Thermococcus litoralis
Mn2+	highest kcat/Km value obtained	Pyrococcus horikoshii
additional information	ADP-dependent kinase is regulated by divalent metal cations due to binding of this ligand to a second site. Results show that a complex between a divalent metal cation and the nucleotide is required for the phosphoryl transfer reaction. The presence of a second metal binding site is suggested which regulates the activity by producing an enzyme with a reduced catalytic constant	Pyrococcus furiosus
additional information	ADP-dependent kinase is regulated by divalent metal cations due to binding of this ligand to a second site. Results show that a complex between a divalent metal cation and the nucleotide is required for the phosphoryl transfer reaction. The presence of a second metal binding site is suggested which regulates the activity by producing an enzyme with a reduced catalytic constant	Pyrococcus horikoshii
additional information	ADP-dependent kinase is regulated by divalent metal cations due to binding of this ligand to a second site. Results show that a complex between a divalent metal cation and the nucleotide is required for the phosphoryl transfer reaction. The presence of a second metal binding site is suggested which regulates the activity by producing an enzyme with a reduced catalytic constant	Thermococcus litoralis

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus furiosus	-	-	-
Pyrococcus horikoshii	-	-	-
Thermococcus litoralis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ADP + D-fructose	ADP-dependent kinase is regulated by divalent metal cations due to binding of this ligand to a second site. Results show that a complex between a divalent metal cation and the nucleotide is required for the phosphoryl transfer reaction. The presence of a second metal binding site is suggested which regulates the activity by producing an enzyme with a reduced catalytic constant	Pyrococcus horikoshii	AMP + D-fructose 6-phosphate	-	?
ADP + D-glucose	ADP-dependent kinase is regulated by divalent metal cations due to binding of this ligand to a second site. Results show that a complex between a divalent metal cation and the nucleotide is required for the phosphoryl transfer reaction. The presence of a second metal binding site is suggested which regulates the activity by producing an enzyme with a reduced catalytic constant	Pyrococcus furiosus	AMP + D-glucose 6-phosphate	-	?
ADP + D-glucose	ADP-dependent kinase is regulated by divalent metal cations due to binding of this ligand to a second site. Results show that a complex between a divalent metal cation and the nucleotide is required for the phosphoryl transfer reaction. The presence of a second metal binding site is suggested which regulates the activity by producing an enzyme with a reduced catalytic constant	Thermococcus litoralis	AMP + D-glucose 6-phosphate	-	?

Synonyms

Synonyms	Comment	Organism
pfGK	-	Pyrococcus furiosus
PhPFK	-	Pyrococcus horikoshii
tlGK	-	Thermococcus litoralis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
40	-	assay at	Pyrococcus furiosus
40	-	assay at	Thermococcus litoralis
50	-	assay at	Pyrococcus horikoshii

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
21	-	ADP	in the presence of 1 mM Mn2+, pH 7.8, 40°C	Thermococcus litoralis
35	-	ADP	in the presence of 1 mM Mg2+, pH 7.8, 40°C	Thermococcus litoralis
44	-	ADP	in the presence of 1 mM Co2+, pH 7.8, 40°C	Thermococcus litoralis
52	-	ADP	in the presence of 1 mM Mg2+, pH 6.5, 50°C	Pyrococcus horikoshii
67	-	ADP	in the presence of 1 mM Mn2+, pH 6.5, 50°C	Pyrococcus horikoshii
98	-	ADP	in the presence of 1 mM Co2+, pH 6.5, 50°C	Pyrococcus horikoshii
104	-	ADP	in the presence of 1 mM Mg2+, pH 7.8, 40°C	Pyrococcus furiosus
114	-	ADP	in the presence of 1 mM Co2+, pH 7.8, 40°C	Pyrococcus furiosus
116	-	ADP	in the presence of 1 mM Mn2+, pH 7.8, 40°C	Pyrococcus furiosus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.5	-	assay at	Pyrococcus furiosus
6.5	-	assay at	Pyrococcus horikoshii
6.5	-	assay at	Thermococcus litoralis

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.3	-	ADP	pH 7.8, 40°C	Thermococcus litoralis
0.58	-	ADP	pH 7.8, 40°C	Pyrococcus furiosus
3.4	-	ADP	pH 6.5, 40°C	Pyrococcus horikoshii

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
1200	-	ADP	in the presence of 1 mM Mn2+, pH 7.8, 40°C	Thermococcus litoralis
1500	-	ADP	in the presence of 1 mM Mg2+, pH 7.8, 40°C	Thermococcus litoralis
2900	-	ADP	in the presence of 1 mM Co2+, pH 7.8, 40°C	Thermococcus litoralis
4400	-	ADP	in the presence of 1 mM Co2+, pH 6.5, 50°C	Pyrococcus horikoshii
4600	-	ADP	in the presence of 1 mM Co2+, pH 7.8, 40°C	Pyrococcus furiosus
5300	-	ADP	in the presence of 1 mM Mn2+, pH 7.8, 40°C	Pyrococcus furiosus
6500	-	ADP	in the presence of 1 mM Mg2+, pH 6.5, 50°C	Pyrococcus horikoshii
7400	-	ADP	in the presence of 1 mM Mg2+, pH 7.8, 40°C	Pyrococcus furiosus
8400	-	ADP	in the presence of 1 mM Mn2+, pH 6.5, 50°C	Pyrococcus horikoshii

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Release 2023.1 (January 2023)