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Information on EC 2.7.1.1 - hexokinase and Organism(s) Sulfurisphaera tokodaii and UniProt Accession Q96Y14

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EC Tree
IUBMB Comments
D-Glucose, D-mannose, D-fructose, sorbitol and D-glucosamine can act as acceptors; ITP and dATP can act as donors. The liver isoenzyme has sometimes been called glucokinase.
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This record set is specific for:
Sulfurisphaera tokodaii
UNIPROT: Q96Y14
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The taxonomic range for the selected organisms is: Sulfurisphaera tokodaii
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
hexokinase, hexokinase ii, hexokinase 2, hexokinase i, hk ii, hxk, liver glucokinase, hexokinase 1, hexokinase-2, hkdc1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP-dependent hexokinase
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STK_23540
locus name
ATP-D-hexose 6-phosphotransferase
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ATP-dependent hexokinase
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brain form hexokinase
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glucokinase
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glucose ATP phosphotransferase
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hexokinase (phosphorylating)
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hexokinase D
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hexokinase PI
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hexokinase PII
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hexokinase type IV
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hexokinase type IV glucokinase
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hexokinase, tumor isozyme
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HK
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HK4
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HXK
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kinase, hexo- (phosphorylating)
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muscle form hexokinase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-hexose 6-phosphotransferase
D-Glucose, D-mannose, D-fructose, sorbitol and D-glucosamine can act as acceptors; ITP and dATP can act as donors. The liver isoenzyme has sometimes been called glucokinase.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-51-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
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-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
show the reaction diagram
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-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
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-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
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-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
81% of the activity with ATP
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-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
show the reaction diagram
52% of the activity with ATP
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?
ITP + D-glucose
IDP + D-glucose 6-phosphate
show the reaction diagram
64% of the activity with ATP
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?
UTP + D-glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
37% of the activity with ATP
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?
additional information
?
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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
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
in Sulfolobus tokodaii this is the sole enzyme responsible for the phosphorylation of glucose in vivo
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
no activity is detected without a divalent cation. 100, 153, and 80% relative activity in the presence of Mg2+, Co2+, and Mn2+, respectively, at 4 mM
Mn2+
no activity is detected without a divalent cation. 100, 153, and 80% relative activity in the presence of Mg2+, Co2+, and Mn2+, respectively, at 4 mM
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
1 mM, 92% inhibition. Competitive inhibition versus ATP, noncompetitive inhibition versus D-glucose
AMP
1 mM, 73% inhibition
CDP
1 mM, 33% inhibition
D-fructose 6-phosphate
10 mM, 33% inhibition
diphosphate
10 mM, 54% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.44
2-deoxy-D-glucose
pH 7.5, 50°C, ATP as phosphoryl donor
0.12
ATP
pH 7.5, 50°C, D-glucose as phosphoryl acceptor
0.52
CTP
pH 7.5, 50°C, D-glucose as phosphoryl acceptor
30
D-fructose
pH 7.5, 50°C, ATP as phosphoryl donor
0.23
D-glucosamine
pH 7.5, 50°C, ATP as phosphoryl donor
0.05
D-glucose
pH 7.5, 50°C, ATP as phosphoryl donor
0.13
D-mannose
pH 7.5, 50°C, ATP as phosphoryl donor
0.32
N-acetyl-D-glucosamine
pH 7.5, 50°C, ATP as phosphoryl donor
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
170
2-deoxy-D-glucose
pH 7.5, 50°C
259
ATP
pH 7.5, 50°C
52
CTP
pH 7.5, 50°C
1.4
D-fructose
pH 7.5, 50°C
247
D-glucosamine
pH 7.5, 50°C
717
D-glucose
pH 7.5, 50°C
420
D-mannose
pH 7.5, 50°C
100
N-acetyl-D-glucosamine
pH 7.5, 50°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018
ADP
pH 7.5, 50°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26
pH 7.5, 50°C, substrate: D-glucose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
more than 60% of the maximal activity in the pH range of 6.5 to 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
2 * 32000, SDS-PAGE
32100
2 * 32100, calculated from sequence
64000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method at 25°C. Crystal structures of StHK in four different forms: (i) apo-form, (ii) binary complex with glucose, (iii) binary complex with ADP, and (iv) quaternary complex with xylose, Mg2+, and ADP. Forms i and iii are in the open state, and forms ii and iv are in the closed state, indicating that sugar binding induces a large conformational change, whereas ADP binding does not
hanging drop vapor diffusion method. Crystal structures of StHK in four different forms: (i) apo-form, (ii) binary complex with glucose, (iii) binary complex with ADP, and (iv) quaternary complex with xylose, Mg2+, and ADP. Forms i and iii are in the open state, and forms ii and iv are in the closed state, indicating that sugar binding induces a large conformational change, whereas ADP binding does not
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
pH 7.5, 120 min, 14% loss of activity
90
pH 7.5, 120 min, 80% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nishimasu, H.; Fushinobu, S.; Shoun, H.; Wakagi, T.
Identification and characterization of an ATP-dependent hexokinase with broad substrate specificity from the hyperthermophilic archaeon Sulfolobus tokodaii
J. Bacteriol.
188
2014-2019
2006
Sulfurisphaera tokodaii (Q96Y14), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7 (Q96Y14)
Manually annotated by BRENDA team
Nishimasu, H.; Fushinobu, S.; Shoun, H.; Wakagi, T.
Crystal structures of an ATP-dependent hexokinase with broad substrate specificity from the hyperthermophilic archaeon Sulfolobus tokodaii
J. Biol. Chem.
282
9923-9931
2007
Sulfurisphaera tokodaii (Q96Y14), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7 (Q96Y14)
Manually annotated by BRENDA team