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Information on EC 2.7.1.147 - ADP-specific glucose/glucosamine kinase and Organism(s) Thermococcus litoralis and UniProt Accession Q7M537

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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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Thermococcus litoralis
UNIPROT: Q7M537
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The taxonomic range for the selected organisms is: Thermococcus litoralis
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 glucokinase
-
ADP-dependent glucokinase
-
-
-
-
ADP-specific glucokinase
-
-
-
-
ADP:D-glucose 6-phosphotransferase
-
-
-
-
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
-
CDP shows comparable activity
-
-
ir
additional information
?
-
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
-
-
-
?
D-glucose + ADP
D-glucose 6-phosphate + AMP
show the reaction diagram
-
-
-
?
D-glucose + ADP
D-glucose 6-phosphate + AMP
show the reaction diagram
-
CDP shows comparable activity
-
-
ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
enzyme TlGK is not significantly inhibited by D-fructose 6-phosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0086 - 1.46
ADP
0.044 - 109
D-glucose
0.015 - 0.023
ADP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.56 - 58
ADP
42
D-glucose
pH 7.8, 40°C
21 - 44
ADP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.95 - 4140
ADP
0.005 - 954.54
D-glucose
1200 - 2900
ADP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14
D-glucose
pH 7.8, 40°C
0.3
ADP
-
pH 7.8, 40°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
additional information
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
-
1 * 52000
54000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 52000
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.3 A resolution, R-factor of 20.4%
crystal structures of apo form and holo form, in the presence of D-glucose and the nonhydrolyzable ADP analog adenosine 5'-(3-thio)diphosphate. The conformational changes upon sequential substrate binding can be explained by an almost pure rotation (or a rotation plus a translation) facilitated by residues in the flexible inter-domain connection
crystallized with ADP and Mg2+, the structure is determined by multiple isomorphous replacement with anomalous scattering and refined at 2.3 A. Crystals are grown at 25°C by the hanging drop vapor diffusion method
sitting-drop vapor-diffusion crystallization
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E279D
mutation does not affect the KM value for MgADP-, but causes a large increase on KM value for glucose and an 87fold weaker binding of glucose onto the non-hydrolysable enzyme-AMP-AlF3 complex. Mutant is still inhibited by free Mg2+
E279L
mutation does not affect the KM value for MgADP-, but causes a large increase on KM value for glucose and an 87fold weaker binding of glucose onto the non-hydrolysable enzyme-AMP-AlF3 complex. Mutant is still inhibited by free Mg2+
E279Q
mutation does not affect the KM value for MgADP-, but causes a large increase on KM value for glucose and an 87fold weaker binding of glucose onto the non-hydrolysable enzyme-AMP-AlF3 complex. Mutant is still inhibited by free Mg2+
E308Q
mutation increases the KM value for MgADP-, mutant is activated by free Mg2+
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene glkA, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ito, S.; Fushinobu, S.; Yoshioka, I.; Koga, S.; Matsuzawa, H.; Wakagi, T.
Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon
Structure
9
205-214
2001
Thermococcus litoralis (Q7M537), Thermococcus litoralis
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
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
Rivas-Pardo, J.A.; Herrera-Morande, A.; Castro-Fernandez, V.; Fernandez, F.J.; Vega, M.C.; Guixe, V.
Crystal structure, SAXS and kinetic mechanism of hyperthermophilic ADP-dependent glucokinase from Thermococcus litoralis reveal a conserved mechanism for catalysis
PLoS One
8
e66687
2013
Thermococcus litoralis (Q7M537), Thermococcus litoralis, Thermococcus litoralis DSM 5473 (Q7M537)
Manually annotated by BRENDA team
Abarca-Lagunas, M.J.; Rivas-Pardo, J.A.; Ramirez-Sarmiento, C.A.; Guixe, V.
Dissecting the functional roles of the conserved NXXE and HXE motifs of the ADP-dependent glucokinase from Thermococcus litoralis
FEBS Lett.
589
3271-3276
2015
Thermococcus litoralis (Q7M537), Thermococcus litoralis, Thermococcus litoralis DSM 5473 (Q7M537)
Manually annotated by BRENDA team
Ito, S.; Fushinobu, S.; Yoshioka, I.; Koga, S.; Matsuzawa, H.; Wakagi, T.
Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon
Structure
9
205-214
2001
Thermococcus litoralis (Q7M537), Thermococcus litoralis, Thermococcus litoralis DSM 5473 (Q7M537)
Manually annotated by BRENDA team
Castro-Fernandez, V.; Herrera-Morande, A.; Zamora, R.; Merino, F.; Gonzalez-Ordenes, F.; Padilla-Salinas, F.; Pereira, H.M.; Brandao-Neto, J.; Garratt, R.C.; Guixe, V.
Reconstructed ancestral enzymes reveal that negative selection drove the evolution of substrate specificity in ADP-dependent kinases
J. Biol. Chem.
292
15598-15610
2017
Methanocaldococcus jannaschii (Q58999), Methanocaldococcus jannaschii ATCC 43067 (Q58999), Thermococcus litoralis (Q7M537), Thermococcus litoralis ATCC 51850 (Q7M537), uncultured bacterium
Manually annotated by BRENDA team