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Information on EC 2.7.1.1 - hexokinase and Organism(s) Bos taurus and UniProt Accession Q5W5U3

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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:
Bos taurus
UNIPROT: Q5W5U3
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The taxonomic range for the selected organisms is: Bos taurus
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
hexokinase type I
-
ATP-D-hexose 6-phosphotransferase
-
-
-
-
ATP-dependent hexokinase
-
-
-
-
brain form hexokinase
-
-
-
-
glucokinase
-
-
-
-
glucose ATP phosphotransferase
-
-
-
-
hexokinase (phosphorylating)
-
-
-
-
hexokinase D
-
-
-
-
hexokinase PI
-
-
-
-
hexokinase PII
-
-
-
-
hexokinase type IV
-
-
-
-
hexokinase type IV glucokinase
-
-
-
-
hexokinase, tumor isozyme
-
-
-
-
HK
-
-
-
-
HK4
-
-
-
-
HXK
-
-
-
-
kinase, hexo- (phosphorylating)
-
-
-
-
muscle form hexokinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
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
-
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-2-fluoro-D-glucose
ADP + 2-deoxy-2-fluoro-D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
2-fluoro-2-deoxy-D-glucose + ATP
2-fluoro-2-deoxy-D-glucose 6-phosphate + ADP
show the reaction diagram
-
-
-
?
ATP + 2-deoxy-2-fluoro-D-glucose
ADP + 2-deoxy-2-fluoro-D-glucose 6-phosphate
show the reaction diagram
-
good substrate
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 5-thio-D-glucose
ADP + 5-thio-D-glucose 6-phosphate
show the reaction diagram
-
very slow phosphorylation
-
-
?
ATP + D-mannosamine
ADP + D-mannosamine 6-phosphate
show the reaction diagram
-
fairly good substrate
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
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
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
involved in glucose catabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
MgATP2-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
MgATP2-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-Glucose 1,6-bisphosphate
competitive versus MgATP2-, low concentration of phosphate counteract
D-glucose 6-phosphate
competitive versus MgATP2-
1,5-Anhydro-D-glucitol 6-phosphate
-
hexokinase bound at type A and type B sites of brain mitochondria is relatively insensitive, hexokinase bound at type B sites, after removal of enzyme of type A sites, shows increased sensitivity
5-thio-D-glucose
-
-
additional information
-
enzymes from rat brain and bovine heart are not inhibited by palmitoyl-CoA or regulatory protein
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.67 - 0.98
ATP
0.047 - 0.072
D-glucose
0.2
2-deoxy-2-fluoro-D-glucose
-
at 37°C, pH 7.4
0.125 - 0.152
2-deoxy-D-glucose
0.055 - 0.062
2-fluoro-2-deoxy-D-glucose
-
HK I, at 25°C, pH 7.4
0.032 - 0.034
D-glucose
-
HK I, at 25°C, pH 7.4
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033 - 0.036
D-Glucose 1,6-bisphosphate
0.045 - 0.066
D-glucose 6-phosphate
0.1
5-thio-D-glucose
-
inhibition of fructose phosphorylation, at 37°C, pH 7.4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.44
cell extract of recombinant Escherichia coli expressing the full length enzyme
141
purified recombinant catalytic C-terminal domain of the enzyme
3.5
cell extract of recombinant Escherichia coli expressing the catalytic C-terminal domain of the enzyme
94
purified recombinant full length enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
hexokinase I, predominant in normal brain
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
bound at type A sites and type B sites of brain mitochondria, ratio of type A:type B is 40:60, enzyme bound at type A sites is releaved by glucose 6-phosphate, but not that of type B sites
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q5W5U3_BOVIN
917
0
102207
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
111000
x * 111000, recombinant full length enzyme, SDS-PAGE, x * 56000, recombinant catalytic C-terminal domain, SDS-PAGE
56000
x * 111000, recombinant full length enzyme, SDS-PAGE, x * 56000, recombinant catalytic C-terminal domain, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 111000, recombinant full length enzyme, SDS-PAGE, x * 56000, recombinant catalytic C-terminal domain, SDS-PAGE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant full length enzyme and C-terminal domain from Escherichia coli strain BL21(DE3) by ion exchange, hydrophobic interaction, anddye ligand affinity chromatography, and gel filtration
partial
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
type I enzyme, DNA and amino acid sequence determination and analysis, functional expression of soluble full length enzyme and of the soluble C-terminal domain in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vandercammen, A.; Van Schaftingen, E.
Competitive inhibition of liver glucokinase by its regulatory protein
Eur. J. Biochem.
200
545-551
1991
Bos taurus, Rhinella marina, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Machado de Domenech, E.E.; Sols, A.
Specificity of hexokinases towards some uncommon substrates and inhibitors
FEBS Lett.
119
174-176
1980
Bos taurus, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Muzi, M.; Freeman, S.D.; Burrows, R.C.; Wiseman, R.W.; Link, J.M.; Krohn, K.A.; Graham, M.M.; Spence, A.M.
Kinetic characterization of hexokinase isoenzymes from glioma cells: Implications for FDG imaging of human brain tumors
Nucl. Med. Biol.
28
107-116
2001
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Cesar, M.deC.; Wilson, J.E.
Functional characteristics of hexokinase bound to the type A and type B sites of bovine brain mitochondria
Arch. Biochem. Biophys.
397
106-112
2002
Bos taurus
Manually annotated by BRENDA team
Andreoni, F.; Serafini, G.; Laguardia, M.E.; Magnani, M.
Bovine hexokinase type I: full-length cDNA sequence and characterisation of the recombinant enzyme
Mol. Cell. Biochem.
268
9-18
2005
Bos taurus (Q5W5U3), Bos taurus
Manually annotated by BRENDA team