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Information on EC 2.7.1.1 - hexokinase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P04807

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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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Saccharomyces cerevisiae
UNIPROT: P04807
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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-D-hexose 6-phosphotransferase
-
-
-
-
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
-
-
-
-
HK4
-
-
-
-
HXK
-
-
-
-
kinase, hexo- (phosphorylating)
-
-
-
-
muscle form hexokinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + D-hexose = ADP + D-hexose 6-phosphate
show the reaction diagram
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 + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
ATP + 1,5-anhydro-D-glucitol
ADP + 1,5-anhydro-D-glucitol 6-phosphate
show the reaction diagram
-
weak
-
-
?
ATP + 1-thio-D-glucose
ADP + 1-thio-D-glucose 6-phosphate
show the reaction diagram
-
isoenzyme II, weak
-
-
?
ATP + 2-deoxy-2-fluoro-D-glucose
ADP + 2-deoxy-2-fluoro-D-glucose 6-phosphate
show the reaction diagram
-
good substrate
-
-
?
ATP + 3-deoxy-3-amino-D-glucose
ADP + 3-deoxy-3-amino-D-glucose 6-phosphate
show the reaction diagram
-
isoenzyme II, weak
-
-
?
ATP + 5-thio-D-glucose
ADP + 5-thio-D-glucose 6-phosphate
show the reaction diagram
-
very slow phosphorylation
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
ATP + D-mannosamine
ADP + D-mannosamine 6-phosphate
show the reaction diagram
-
fairly good substrate
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
-
35% of the activity with ATP
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
hexokinase isoenzymes are particularly important in glycolytic flux and, in addition, hexokinase PII, hexokinase PIIM or both are also responsible for the overall regulation of carbohydrate metabolism, role in glucose repression
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
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-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
hexokinase isoenzymes are particularly important in glycolytic flux and, in addition, hexokinase PII, hexokinase PIIM or both are also responsible for the overall regulation of carbohydrate metabolism, role in glucose repression
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-bromo-2-oxopropionic acid
-
-
6-deoxy-D-glucose
-
-
ADP
-
competitive versus ATP, inhibition mode, 91.3% decreased activity
AMP
-
51.4% decreased activity
ATP
-
isoenzymes PII and PIIM are strongly inhibited by high physiological concentrations, 5 mM: 50% inhibition
CoA
-
54.1% decreased activity
D-glucose 1,6-diphosphate
-
15.7% decreased activity
D-glucose 6-phosphate
-
54.3% decreased activity
D-mannose
D-xylose
-
irreversible inactivation of the 3 isoenzymes, hexokinase PI inactivation requires ATP, hexokinase PII is inactivated by D-xylose without ATP, glucokinase is protected by ATP, competitive inhibitor of hexokinase PI and glucokinase, non-competitive inhibitor of hexokinase PII
GDP
-
31.3% decreased activity
Mg2+
-
uncomplexed
N-acetylmannosamine
-
-
Ni2+
-
competitive versus ATP via replacement of Mg2+, noncompetitive versus D-glucose via a cysteine residue proximal to the D-glucose binding site, enzyme-nickel interactions with positive cooperativity via histidine residues, no saturation is reached, nickel binding induces conformational changes in the secondary structure of the enzyme modifying the monomer/dimer equilibrium and decreasing the activity, overview
oxidized glutathione
-
82.9% decreased activity
reduced glutathione
-
54.5% decreased activity
S-nitrosoglutathione
hexokinase is particularly susceptible to protein structure modifications when exposed to even low concentrations of S-nitrosoglutathione. Biologically relevant [S-nitrosoglutathione]/[hexokinase] causes a significant decrease in Vmax with glucose (but not with fructose), along with oxidation of 5 Met and nitration of 4 Tyr. Preincubation of hexokinase with glucose abrogates the effect of S-nitrosoglutathione whereas fructose is ineffective
trehalose 6-phosphate
-
90.9% decreased activity
Triethyltin bromide
-
selective inhibitor, sugar substrates D-glucose and D-mannose protect
UDP
-
51.9% decreased activity
UDP-glucose
-
62.5% decreased activity
xylose
irreversible inactivation
additional information
-
multiplex inhibitor screening, mass spectrometry-based assay
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-phosphoglycerate
-
activates
citrate
-
allosteric activator
phosphate
-
activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
1,5-anhydro-D-glucitol
-
at 37°C, pH 7.4
5
1-thio-D-glucose
-
at 37°C, pH 7.4
0.2
2-deoxy-2-fluoro-D-glucose
-
at 37°C, pH 7.4
30
3-deoxy-3-amino-D-glucose
-
at 37°C, pH 7.4
4
5-thio-D-glucose
-
-
0.1
ATP
-
pH 7.5, 22°C
0.33 - 2.9
D-fructose
0.04 - 0.47
D-glucose
5
D-mannosamine
-
at 37°C, pH 7.4
0.04
D-mannose
-
glucokinase
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.06 - 1.67
D-glucose
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.99
3-bromo-2-oxopropionic acid
-
-
50
6-deoxy-D-glucose
-
at 37°C, pH 7.4
0.122
ADP
-
pH 7.5, 22°C, versus ATP, dependennt on Mg2+ concentration
0.06
D-mannose
-
glucokinase
0.85 - 80
D-xylose
50
N-acetylmannosamine
-
at 37°C, pH 7.4
4.87 - 9.97
Ni2+
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.39
3-bromo-2-oxopropionic acid
Saccharomyces cerevisiae
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120
-
commercial preparation
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
-
1 * 54000, both isoenzymes PI and PII, SDS-PAGE
55000 - 60000
-
both isoenzymes PI and PII, FPLC gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
at lower Ni2+ concentration
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
isoenzyme PIIM derives from PII by a posttranslational event
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Crystals are grown in hanging drops, crystal structure of yeast hexokinase PI in complex with glucose and refined it at 2.95 A resolution
isoenzymes PI and PII, large crystals in the native and complexed form with glucose
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F159Y
mutant isolated in a sreen for variants with increased resistance to autophosphorylation by xylose. The mutant has 64% higher catalytic activity in the presence of xylose compared to the wild-type and is expected to be a key component for increasing the productivity of recombinant xylose-fermenting strains for bioethanol production from lignocellulosic feedstocks
additional information
-
hex1 mutants with decreased hexokinase activity, hex2 mutants with increased hexokinase activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NaCl slightly destabilizes the enzyme at pH 3.5 and 38.9°C, conditions for low or no aggregation of the enzyme
the stability and folding of yeast hexokinase isoenzyme ScHxk2 consisting of two domains with a discontinuous peptide sequence is analysed. Thermodynamic and spectroscopic analyses of urea-induced structural transitions indicate a thermodynamically stable folding intermediate, which is enzymatically inactive. Both structural domains are partially denatured in this central intermediate, even though tryptophan fluorescence, dynamic light scattering (DLS) and one-dimensional 1H NMR indicate a still compact but non-native structure
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified isoenzymes PI and PII, 25 mM piperazine-HCl, pH 6.5, 50% glycerol, at least several months, minor loss of activity
-
4°C, polybuffer, over 8 days, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3 isoenzymes PI, PII and glucokinase, partial
-
affinity chromatography
-
from overproducing strain
-
isoenzymes PI and PII
-
isoenzymes PI, PII and PIIM
-
kinetic-based biospecific affinity chromatographic studies
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Lycopersicon esculentum
HXK I and HXK II are the structural genes of hexokinase PI and PII
-
HXK I and HXK II hexokinase genes are cloned
-
overexpression of HXK1 in a laboratory strain of Saccharomyces cerevisiae (W303-1A) accelerates fructose consumption more than glucose consumption, but overexpression in a wine yeast strain (VIN13) reduces fructose consumption less than glucose consumption
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jacob, L.; Beecken, V.; Bartunik, L.J.
Purification and crystallization of yeast hexokinase isoenzymes. Characterization of different forms by chromatofocusing
J. Chromatogr.
587
85-92
1991
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Herrero, R.F.P.; Moreno, F.
Inhibition and inactivation of glucose-phosphorylating enzymes from Saccharomyces cerevisiae by D-xylose
J. Gen. Microbiol.
131
2705-2709
1985
Saccharomyces cerevisiae, Saccharomyces cerevisiae G-517 / CECT 1317
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
Siebenlist, K.R.; Taketa, F.
Inhibition of red cell and yeast hexokinase by triethyltin bromide [(C2H5)3SnBr]
Biochem. Biophys. Res. Commun.
95
758-764
1980
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Kopetzki, E.; Entian, K.D.
Purification of yeast hexokinase isoenzymes using affinity chromatography and chromatofocusing
Anal. Biochem.
121
181-185
1982
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Kopetzki, E.; Entian, K.D.
Glucose repression and hexokinase isoenzymes in yeast. Isolation and characterization of a modified hexokinase PII isoenzyme
Eur. J. Biochem.
146
657-662
1985
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Mulcahy, P.; O'Flaherty, M.; Jennings, L.; Griffin, T.
Application of kinetic-based biospecific affinity chromatographic systems to ATP-dependent enzymes: Studies with yeast hexokinase
Anal. Biochem.
309
279-292
2002
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Gao, H.; Leary, J.A.
Multiplex inhibitor screening and kinetic constant determinations for yeast hexokinase using mass spectrometry based assays
J. Am. Soc. Mass Spectrom.
14
173-181
2003
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Kumar, D.P.; Tiwari, A.; Bhat, R.
Effect of pH on the stability and structure of yeast hexokinase A. Acidic amino acid residues in the cleft region are critical for the opening and the closing of the structure
J. Biol. Chem.
279
32093-32099
2004
Saccharomyces cerevisiae (P04807), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Romero, C.S.; Olmo, R.; Teijon, C.; Blanco, M.D.; Teijon, J.M.; Romero, A.
Structural and functional implications of the hexokinase-nickel interaction
J. Inorg. Biochem.
99
2395-2402
2005
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Miller, S.; Ross-Inta, C.; Giulivi, C.
Kinetic and proteomic analyses of S-nitrosoglutathione-treated hexokinase A: consequences for cancer energy metabolism
Amino Acids
32
593-602
2007
Saccharomyces cerevisiae (P04806), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Olsen, S.N.; Ramlov, H.; Westh, P.
Effects of osmolytes on hexokinase kinetics combined with macromolecular crowding Test of the osmolyte compatibility hypothesis towards crowded systems
Comp. Biochem. Physiol. A
148
339-345
2007
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Claeyssen, E.; Rivoal, J.
Isozymes of plant hexokinase: occurrence, properties and functions
Phytochemistry
68
709-731
2007
Saccharomyces cerevisiae, Solanum lycopersicum, Pisum sativum, Solanum tuberosum, Solanum tuberosum (O64390), Solanum tuberosum (Q9SQ76), Triticum aestivum, Zea mays, Solanum chacoense, Capsicum chacoense, Arabidopsis thaliana (Q9FZG4), Arabidopsis thaliana
Manually annotated by BRENDA team
Gharbi, I.; Ricard, B.; Rolin, D.; Maucourt, M.; Andrieu, M.H.; Bizid, E.; Smiti, S.; Brouquisse, R.
Effect of hexokinase activity on tomato root metabolism during prolonged hypoxia
Plant Cell Environ.
30
508-517
2007
Solanum lycopersicum, Saccharomyces cerevisiae (P04807), Saccharomyces cerevisiae, Arabidopsis thaliana (Q42525)
Manually annotated by BRENDA team
Berthels, N.J.; Cordero Otero, R.R.; Bauer, F.F.; Pretorius, I.S.; Thevelein, J.M.
Correlation between glucose/fructose discrepancy and hexokinase kinetic properties in different Saccharomyces cerevisiae wine yeast strains
Appl. Microbiol. Biotechnol.
77
1083-1091
2008
Saccharomyces cerevisiae (P04806), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Kuser, P.; Cupri, F.; Bleicher, L.; Polikarpov, I.
Crystal structure of yeast hexokinase PI in complex with glucose: A classical "induced fit" example revised
Proteins
72
731-740
2008
Saccharomyces cerevisiae (P04806), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Wang, T.; Kang, J.
Hexokinase inhibitor screening based on adenosine 5-diphosphate determination by electrophoretically mediated microanalysis
Electrophoresis
30
1349-1354
2009
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Lilie, H.; Baer, D.; Kettner, K.; Weininger, U.; Balbach, J.; Naumann, M.; Mueller, E.C.; Otto, A.; Gast, K.; Golbik, R.; Kriegel, T.
Yeast hexokinase isoenzyme ScHxk2: stability of a two-domain protein with discontinuous domains
Protein Eng. Des. Sel.
24
79-87
2011
Saccharomyces cerevisiae (P04807), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Bergdahl, B.; Sandstroem, A.G.; Borgstroem, C.; Boonyawan, T.; van Niel, E.W.; Gorwa-Grauslund, M.F.
Engineering yeast hexokinase 2 for improved tolerance toward xylose-induced inactivation
PLoS ONE
8
e75055
2013
Saccharomyces cerevisiae (P04806), Saccharomyces cerevisiae
Manually annotated by BRENDA team