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Information on EC 2.7.1.147 - ADP-specific glucose/glucosamine kinase and Organism(s) Pyrococcus furiosus and UniProt Accession Q9V2Z6

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IUBMB Comments
Requires Mg2+. The enzyme, characterized from a number of hyperthermophilic archaeal species, is highly specific for ADP. No activity is detected when ADP is replaced by ATP, GDP, phosphoenolpyruvate, diphosphate or polyphosphate.
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Pyrococcus furiosus
UNIPROT: Q9V2Z6
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The taxonomic range for the selected organisms is: Pyrococcus furiosus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
adpgk, adp-dependent glucokinase, adp-pfk, adp-dependent kinase, tk1110, adp-gk, phpfk, adp-dependent hexokinase, adp-hk, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ADP-dependent kinase
-
ADP-dependent glucokinase
-
-
-
-
ADP-dependent hexokinase
-
-
ADP-specific glucokinase
-
-
-
-
ADP:D-glucose 6-phosphotransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ADP + D-glucose = AMP + D-glucose 6-phosphate
show the reaction diagram
reaction mechanism, the catalytic base Asp451 is essential
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho-group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ADP:D-glucose/D-glucosamine 6-phosphotransferase
Requires Mg2+. The enzyme, characterized from a number of hyperthermophilic archaeal species, is highly specific for ADP. No activity is detected when ADP is replaced by ATP, GDP, phosphoenolpyruvate, diphosphate or polyphosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
173585-07-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + D-glucose
AMP + D-glucose 6-phosphate
show the reaction diagram
D-glucose + ADP
D-glucose 6-phosphate + AMP
show the reaction diagram
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
show the reaction diagram
-
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
-
-
?
D-1,5-anhydroglucitol + ADP
?
show the reaction diagram
-
-
-
-
?
D-glucose + ADP
D-glucose 6-phosphate + AMP
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + D-glucose
AMP + D-glucose 6-phosphate
show the reaction diagram
step of the Embden-Meyerhoff pathway
-
-
?
D-glucose + ADP
D-glucose 6-phosphate + AMP
show the reaction diagram
-
-
-
?
D-glucose + ADP
D-glucose 6-phosphate + AMP
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
binding site structure
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
binding site structure
Ca2+
-
17% of activity
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
strong competitive inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014 - 0.025
ADP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
104 - 116
ADP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4600 - 7400
ADP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
AMP
versus ADP
0.58
ADP
-
pH 7.8, 40°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
89000
gel filtration
100000
-
gel filtration
93000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with AMP, sitting drop vapour diffusion method, 10 mg/ml protein in 6 mM ADP-beta-S, 30 mM glucose mixed in equal volumes with reservoir solution containing 1.6 M citrate, pH 6.5, 10 mM DTT, equilibration against 0.075 ml of reservoir solution at 25°C, a few weeks to 1 month, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement, modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C174S
site-directed mutagenesis, activity and oligomarization state are similar to the wild-type enzyme
C94S
site-directed mutagenesis, activity is similar to the wild-type enzyme, the mutant enzyme forms no dimers, but monomers
C94S/C174S
site-directed mutagenesis, activity is similar to the wild-type enzyme, the mutant enzyme forms no dimers, but monomers
D451A
site-directed mutagenesis, nearly inactive mutant
D451N
site-directed mutagenesis, nearly inactive mutant
D451S
site-directed mutagenesis, nearly inactive mutant
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
stable for 220 min
90
-
at least stable for 10 min
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) by heat treatment at 90°C, ammonium sulfate fractionation, ion exchange chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli
-
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kengen, S.W.M.; Tuininga, J.E.; de Bok, F.A.M.; Stams, A.J.M.; de Vos, W.M.
Purification and characterization of a novel ADP-dependent glucokinase from the hyperthermophilic archaeon Pyrococcus furiosus
J. Biol. Chem.
270
30453-30457
1995
Pyrococcus furiosus
Manually annotated by BRENDA team
Kengen, S.W.M.; Tuininga, J.E.; Verhees, C.H.; Van der Oost, J.; Stams, A.J.M.; De Vos, W.M.
ADP-dependent glucokinase and phosphofructokinase from Pyrococcus furiosus
Methods Enzymol.
331
41-53
2001
Pyrococcus furiosus
Manually annotated by BRENDA team
Koga, S.; Yoshioka, I.; Sakuraba, H.; Takahashi, M.; Sakasegawa, S.; Shimizu, S.; Ohshima, T.
Biochemical characterization, cloning, and sequencing of ADP-dependent (AMP-forming) glucokinase from two hyperthermophilic archaea, Pyrococcus furiosus and Thermococcus litoralis
J. Biochem.
128
1079-1085
2000
Pyrococcus furiosus, Thermococcus litoralis
Manually annotated by BRENDA team
Verhees, C.H.; Koot, D.G.; Ettema, T.J.; Dijkema, C.; De Vos, W.M.; Van Der Oost, J.
Biochemical adaptations of two sugar kinases from the hyperthermophilic archaeon Pyrococcus furiosus
Biochem. J.
366
121-127
2002
Pyrococcus furiosus (Q9V2Z6), Pyrococcus furiosus
Manually annotated by BRENDA team
Ito, S.; Fushinobu, S.; Jeong, J.J.; Yoshioka, I.; Koga, S.; Shoun, H.; Wakagi, T.
Crystal structure of an ADP-dependent glucokinase from Pyrococcus furiosus: implications for a sugar-induced conformational change in ADP-dependent kinase
J. Mol. Biol.
331
871-883
2003
Pyrococcus furiosus (Q9V2Z6), Pyrococcus furiosus
Manually annotated by BRENDA team
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
Biochimie
94
516-524
2012
Pyrococcus furiosus, Pyrococcus horikoshii, Thermococcus litoralis
Manually annotated by BRENDA team
Kengen, S.W.; de Bok, F.A.; van Loo, N.D.; Dijkema, C.; Stams, A.J.; de Vos, W.M.
Evidence for the operation of a novel Embden-Meyerhof pathway that involves ADP-dependent kinases during sugar fermentation by Pyrococcus furiosus
J. Biol. Chem.
269
17537-17541
1994
Pyrococcus furiosus
Manually annotated by BRENDA team