Information on EC 2.7.1.1 - hexokinase

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The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.7.1.1
-
RECOMMENDED NAME
GeneOntology No.
hexokinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + D-hexose = ADP + D-hexose 6-phosphate
show the reaction diagram
equilibrium random Bi Bi mechanism with formation of the abortive enzyme-ADP-glucose complex
-
ATP + D-hexose = ADP + D-hexose 6-phosphate
show the reaction diagram
-
-
-
-
ATP + D-hexose = ADP + D-hexose 6-phosphate
show the reaction diagram
rapid random kinetic mechanism, erythrocyte enzyme and hexokinase I
-
ATP + D-hexose = ADP + D-hexose 6-phosphate
show the reaction diagram
random kinetic mechanism
-
ATP + D-hexose = ADP + D-hexose 6-phosphate
show the reaction diagram
random process
-
ATP + D-hexose = ADP + D-hexose 6-phosphate
show the reaction diagram
random sequential mechanism
-
ATP + D-hexose = ADP + D-hexose 6-phosphate
show the reaction diagram
substrate binding mechanism and structure
Q5RLG0, -
ATP + D-hexose = ADP + D-hexose 6-phosphate
show the reaction diagram
non-cooperative conditions shows an ordered kinetic mechanism with MgADP as the last product to be released
-
ATP + D-hexose = ADP + D-hexose 6-phosphate
show the reaction diagram
catalytic residues in the D-glucose binding site are Glu269, Glu302, and Asp211
-
ATP + D-hexose = ADP + D-hexose 6-phosphate
show the reaction diagram
equilibrium random Bi Bi mechanism with formation of the abortive enzyme-ADP-glucose complex
Schizosaccharomyces pombe NCYC 132S2-2
-
-
ATP + D-hexose = ADP + D-hexose 6-phosphate
show the reaction diagram
substrate binding mechanism and structure
Thermus caldophilus GK24
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
Biosynthesis of secondary metabolites
-
Butirosin and neomycin biosynthesis
-
Fructose and mannose metabolism
-
Galactose metabolism
-
Glycolysis / Gluconeogenesis
-
glycolysis VI (metazoan)
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Starch and sucrose metabolism
-
Streptomycin biosynthesis
-
sucrose degradation III (sucrose invertase)
-
trehalose degradation I (low osmolarity)
-
trehalose degradation IV
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6-phosphate glucose kinase
A0SZU9
-
AtHXK1
Q42525
-
ATP-D-hexose 6-phosphotransferase
-
-
-
-
ATP-D-hexose-6-phosphotransferase
-
-
ATP-dependent hexokinase
-
-
-
-
ATP-dependent hexokinase
-
-
ATP-dependent hexokinase
Q96Y14
-
ATP-dependent hexokinase
Sulfolobus tokodaii 7
Q96Y14
-
-
ATP-dependent hexokinase
-
-
ATP: D-glucose 6-phosphotransferase
-
-
ATP: D-hexose 6-phosphotransferase
P35557
-
ATP:D-glucose 6-phosphotransferase
-
-
ATP:D-hexose 6-phosphotransferase
-
-
BmHk
Q56VN6
-
brain form hexokinase
-
-
-
-
GKbeta
-
-
glucokinase
-
-
-
-
glucokinase
-
-
glucokinase
-
-
glucokinase
-
-
glucokinase
P35557
-
glucokinase
-
-
glucokinase
-
-
glucose ATP phosphotransferase
-
-
-
-
HaHXK1
B8K2W7
-
hexokinase
-
-
hexokinase
-
-
hexokinase
-
-
hexokinase
A9RE08, A9RIW3, A9S3H4, A9S9F8, A9SJG4, A9SV13, A9TDS4, A9TLJ2, A9U0F4, A9U189, Q6X271
-
hexokinase
-
-
hexokinase
Trichosporonoides megachiliensis
-
-
hexokinase
-
-
hexokinase (phosphorylating)
-
-
-
-
hexokinase 1
Q42525
-
hexokinase 1
-
-
hexokinase 1
-
-
hexokinase 1
-
-
hexokinase 2
-
-
hexokinase 2
Q6Q8A5
-
hexokinase 2
-
-
hexokinase A
-
-
hexokinase A
P04806
-
hexokinase D
-
-
-
-
hexokinase D
-
-
hexokinase D
-
-
hexokinase Dor
-
-
hexokinase II
-
-
hexokinase II
-
isozyme
hexokinase II
P52789
-
hexokinase II
-
-
hexokinase II
-
-
hexokinase IV
-
-
hexokinase PI
-
-
-
-
hexokinase PI
P04806
-
hexokinase PII
-
-
-
-
hexokinase type I
Q5W5U3
-
hexokinase type I
-
substitutes for glucokinase in hepatomas and in embryonic livers
hexokinase type I
P05708
-
hexokinase type II
-
substitutes for glucokinase in hepatomas and in embryonic livers
hexokinase type II
P27881
-
hexokinase type IV
-
-
-
-
hexokinase type IV
-
-
hexokinase type IV glucokinase
-
-
-
-
hexokinase, tumor isozyme
-
-
-
-
hexokinase-1
Q8LH82
-
hexokinase-1
Q9SEK3
-
hexokinase-10
Q2KNB5
-
hexokinase-2
Q2KNB9
-
hexokinase-4
Q6Z398
-
hexokinase-5
Q5W676
-
hexokinase-6
-
-
hexokinase-7
-
-
hexokinase-8
-
-
hexokinase-9
-
-
hexokinase-like 1
-
-
hGK isoform 1
P35557
-
HK
-
-
-
-
HK II
P52789
-
HK II
-
-
HK II
P27881
-
HK1
Q5W5U3
-
HK1
-, O64390
-
HK2
-, Q9SQ76
-
HK4
-
-
-
-
HKI
-
substitutes for glucokinase in hepatomas and in embryonic livers
HKII
-
isozyme
HKII
-
-
HKII
-
substitutes for glucokinase in hepatomas and in embryonic livers
HPGLK1
Q96VP5
-
HXK
-
-
-
-
HXK II
P52789
-
Hxk1
Q8LH82
-
HXK10
Q2KNB5
-
Hxk2
Q6Q8A5
-
Hxk2
Q2KNB9
-
HXK4
Q6Z398
-
HXK5
Q5W676
-
HXK6
-
-
HXK7
-
-
HXK8
-
-
HXK9
-
-
kinase, hexo- (phosphorylating)
-
-
-
-
LGK2
-
-
liver glucokinase
-
-
liver glucokinase isoform 2
-
-
muscle form hexokinase
-
-
-
-
OsHXK
-
-
OsHXK1
Q8LH82
-
OsHXK10
Q2KNB5
-
OsHXK2
Q2KNB9
-
OsHXK3
Q2KNB4
-
OsHXK4
Q6Z398
-
OsHXK5
Q5W676
-
OsHXK6
Q8LQ68
-
OsHXK7
Q1WM16
-
OsHXK9
Q2KNB7
-
plastid hexokinase
-
-
PpHXK1
Q6X271
-
PpHXK10
A9TDS4
-
PpHXK11
A9TLJ2
-
PpHXK2
A9U189
-
PpHXK3
A9U0F4
-
PpHXK4
A9S3H4
-
PpHXK5
A9SJG4
-
PpHXK6
A9S9F8
-
PpHXK7
A9RIW3
-
PpHXK8
A9RE08
-
PpHXK9
A9SV13
-
Rag5p
P33284
-
ROK hexokinase
Q5SLJ4
-
SoHXK1
Q9SEK3
-
STK_23540
Q96Y14
locus name
STK_23540
Sulfolobus tokodaii 7
Q96Y14
locus name
-
StoHK
Q96Y14
-
StoHK
Sulfolobus tokodaii 7
Q96Y14
-
-
TthHK
Q5SLJ4
-
type II hexokinase
P52789
-
xprF
-
formerly
MODY2 glucokinase
P35557
-
additional information
Q6Q8A5
enzyme is a type A hexokinase
additional information
Q5RLG0
ROK-type, i.e. repressor kinase
additional information
Thermus caldophilus GK24
Q5RLG0
ROK-type, i.e. repressor kinase
-
CAS REGISTRY NUMBER
COMMENTARY
9001-51-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain ATCC 11414
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
hexokinase I
-
-
Manually annotated by BRENDA team
hexokinase II
-
-
Manually annotated by BRENDA team
2 isozymes HKI and HKII
-
-
Manually annotated by BRENDA team
hexokinase I
-
-
Manually annotated by BRENDA team
H, isoenzymes Hex I and Hex II
-
-
Manually annotated by BRENDA team
Beagle, 2-7 years old
-
-
Manually annotated by BRENDA team
recombinant
-
-
Manually annotated by BRENDA team
strain B/TH, identical with Vinca rosea
-
-
Manually annotated by BRENDA team
Catharanthus roseus B/TH
strain B/TH, identical with Vinca rosea
-
-
Manually annotated by BRENDA team
Hex A and Hex C; Samarkand, adult
-
-
Manually annotated by BRENDA team
multiple forms: Hex A, Hex B and Hex C; Samarkand, adult
-
-
Manually annotated by BRENDA team
Drosophila melanogaster Samarkand
Samarkand, adult
-
-
Manually annotated by BRENDA team
strain SFL-3, 2 isoenzymes: HXK1 and HXK2
-
-
Manually annotated by BRENDA team
Entamoeba histolytica SFL-3
strain SFL-3, 2 isoenzymes: HXK1 and HXK2
-
-
Manually annotated by BRENDA team
2 subtypes of hexokinase type I
-
-
Manually annotated by BRENDA team
B-cells
-
-
Manually annotated by BRENDA team
GCK mutation (V62M) identified in two families
-
-
Manually annotated by BRENDA team
hexokinase type III and its catalytically active recombinant carboxyl-domain
-
-
Manually annotated by BRENDA team
hexokinase types I and III
-
-
Manually annotated by BRENDA team
multiple forms: Ia, Ib, Ic
-
-
Manually annotated by BRENDA team
nonaggregating mutant of recombinant hexokinase I
Uniprot
Manually annotated by BRENDA team
recombinant
-
-
Manually annotated by BRENDA team
recombinant hexokinase I
-
-
Manually annotated by BRENDA team
recombinant hexokinase I, expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
recombinantly expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
crabtree-negative yeast, gene RAG5
SwissProt
Manually annotated by BRENDA team
strain C3-41
SwissProt
Manually annotated by BRENDA team
type I, type II, type III, and type IV isozymes
-
-
Manually annotated by BRENDA team
as a model of hepatocellular carcinoma
-
-
Manually annotated by BRENDA team
C3H mice implanted with MH134 cells
-
-
Manually annotated by BRENDA team
newborn mice
-
-
Manually annotated by BRENDA team
cv. Samsun, 3 isozymes: 1 membrane-bound, 2 soluble
-
-
Manually annotated by BRENDA team
isozyme hexokinase 2
SwissProt
Manually annotated by BRENDA team
no activity in Sus scrofa
sperm
-
-
Manually annotated by BRENDA team
methylotrophic yeast
SwissProt
Manually annotated by BRENDA team
2 isoenzymes: mitochondrial HK I and a soluble HK
-
-
Manually annotated by BRENDA team
hexokinase I
-
-
Manually annotated by BRENDA team
hexokinase Ia and Ib
-
-
Manually annotated by BRENDA team
contains 11 hexokinase encoding genes
UniProt
Manually annotated by BRENDA team
bullfrog, hexokinase I
-
-
Manually annotated by BRENDA team
adult male Wistar rats
-
-
Manually annotated by BRENDA team
hexokinase IV or D
-
-
Manually annotated by BRENDA team
hexokinase type I
-
-
Manually annotated by BRENDA team
hexokinase type I; hexokinase type II
-
-
Manually annotated by BRENDA team
hexokinase type I; HK I+, a modified form of HK I
-
-
Manually annotated by BRENDA team
hexokinase type II; Wistar rats
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
recombinant hexokinase type I
SwissProt
Manually annotated by BRENDA team
recombinant hexokinases II and III
-
-
Manually annotated by BRENDA team
Sprague-Dawley albino rats, hexokinases B and C
-
-
Manually annotated by BRENDA team
3 isoenzymes: PI, PII and PIIM: a posttranslational modified PII isoenzyme
-
-
Manually annotated by BRENDA team
haploid strain cat1.S3-14A of genotype a his MAL2-8c MAL3 SUC3, isoenzymes PI and PII
-
-
Manually annotated by BRENDA team
isoenzymes I and II
-
-
Manually annotated by BRENDA team
overproducing transformed strain WAY.10-1C, isoenzymes PI and PII
-
-
Manually annotated by BRENDA team
strain G-517 (CECT 1317), 3 isoenzymes PI, PII and glucokinase
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae G-517
strain G-517 (CECT 1317), 3 isoenzymes PI, PII and glucokinase
-
-
Manually annotated by BRENDA team
recombinant hexokinase
-
-
Manually annotated by BRENDA team
strain NCYC 132S2-2, 2 isozymic forms
-
-
Manually annotated by BRENDA team
strain PB003, hexokinase 1
SwissProt
Manually annotated by BRENDA team
strain PB004, hexokinase 2
SwissProt
Manually annotated by BRENDA team
Schizosaccharomyces pombe NCYC 132S2-2
strain NCYC 132S2-2, 2 isozymic forms
-
-
Manually annotated by BRENDA team
Schizosaccharomyces pombe PB003
strain PB003, hexokinase 1
SwissProt
Manually annotated by BRENDA team
Schizosaccharomyces pombe PB004
strain PB004, hexokinase 2
SwissProt
Manually annotated by BRENDA team
starch-utilizing yeast, strain CBS819, i.e. ATCC2322, 2 isoenzymes: hexokinase and glucokinase
-
-
Manually annotated by BRENDA team
cv. Desiree, 3 isoenzymes: HK1, HK2, HK3
-
-
Manually annotated by BRENDA team
Sulfolobus tokodaii 7
-
UniProt
Manually annotated by BRENDA team
2 enzyme forms: hexokinase type II and type III
-
-
Manually annotated by BRENDA team
2 enzyme forms: hexokinase type II and type III; adult pigs
-
-
Manually annotated by BRENDA team
boar
-
-
Manually annotated by BRENDA team
hexokinase IV
-
-
Manually annotated by BRENDA team
Kra 1, i.e. DSM 2078
SwissProt
Manually annotated by BRENDA team
strain GK24
SwissProt
Manually annotated by BRENDA team
Thermus caldophilus GK24
strain GK24
SwissProt
Manually annotated by BRENDA team
RH strain
GenBank
Manually annotated by BRENDA team
RH strain
GenBank
Manually annotated by BRENDA team
Trichosporonoides megachiliensis
strain SN-G42 and 124A
-
-
Manually annotated by BRENDA team
Trichosporonoides megachiliensis SN-G42
strain SN-G42 and 124A
-
-
Manually annotated by BRENDA team
bloodstream forms, stock 427
-
-
Manually annotated by BRENDA team
hexokinase I
-
-
Manually annotated by BRENDA team
strains Y and EP, similar to hexokinase IV
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
defect in the activation of glucokinase is potential contributing factor to the dysregulation of hepatic glucose metabolism in type 2 diabetes
malfunction
-
heterozygous or homozygous loss of function in the glucokinase gene causes either mild diabetes (maturity onset diabetes of the young type 2 [MODY2]) or severe neo-natal onset diabetes, respectively
malfunction
-
heterozygous inactivating mutations in glucokinase cause maturity-onset diabetes of the young (MODY) subtype glucokinase, characterized by mild fasting hyperglycemia
malfunction
-
knockdown of hexokinase II increases the apoptotic susceptibility of tuberous sclerosis complex 2-deficient cells to serum deprivation
malfunction
A9RE08, A9RIW3, A9S3H4, A9S9F8, A9SJG4, A9SV13, A9TDS4, A9TLJ2, A9U0F4, A9U189, Q6X271
PpHXK3 is able to complement a hexokinase-deficient yeast strain; PpHXK3 is not able to complement a hexokinase-deficient yeast strain
malfunction
-
the repressive effects of glucose and chloramphenicol on LHCB expression are inhibited in plastid hexokinase (phxk) mutants
malfunction
-
depletion of HK2 in GBM cells restores oxidative glucose metabolism and increases sensitivity to cell death inducers such as radiation and temozolomide. Intracranial xenografts of HK2-depleted GBM cells shows decreased proliferation and angiogenesis, but increased invasion, as well as diminished expression of hypoxia inducible factor 1alpha and vascular endothelial growth factor
malfunction
-
after silencing NtHXK1 using RNAi plants show stunted growth and leaf chlorosis; overexpression of NtHXK1 results in elevated glucose phosphorylation activity in leaf extracts or chloroplasts. NtHXK1 is able to complement the glucose-insensitive Arabidopsis mutant gin2-1 suggesting that NtHXK1 can take over glucose sensing functions
malfunction
-
an glucose-dependent root hair morphology is readily observed in Arabidopsis lines that overexpress HKL1 protein and in an HXK1-deficient line, gin2-1. Seedlings of these lines produce bulbous root hairs with an enlarged base after transfer from agar plates with normal medium to plates with 6% glucose. Seedling transfer to plates with 2% glucose plus 1-aminocyclopropane-1-carboxylic acid mimics the high-glucose effect in the HKL1 overexpression line but not in HXK1-deficient line gin2-1; an glucose-dependent root hair morphology is readily observed in Arabidopsis lines that overexpress HKL1 protein and in an HXK1-deficient line, gin2-1. Seedlings of these lines produce bulbous root hairs with an enlarged base after transfer from agar plates with normal medium to plates with 6% glucose. Seedling transfer to plates with 2% glucose plus 1-aminocyclopropane-1-carboxylic acid mimics the high-glucose effect in the HKL1 overexpression line but not in HXK1-deficient line gin2-1; glucose-dependent developmental arrest of hkl1-1 mutants can not be rescued in the presence of 1-aminocyclopropane-1-carboxylic acid; glucose-dependent developmental arrest of hkl1-1 mutants can not be rescued in the presence of 1-aminocyclopropane-1-carboxylic acid
malfunction
-
D-allose activates AtABI5 expression in transgenic gin2 (mutant glucose-insensitive2-1 (gin2), which has a null mutation in the glucose sensor gene of AtHXK1) over-expressing wild-type AtHXK1 but not in gin2 over-expressing the catalytic mutant AtHXK1S177A, indicating that the D-allose phosphorylation by HXK to D-allose 6-phosphate (A6P) is the first step for the up-regulation of AtABI5 gene expression as well as D-allose-induced growth inhibition; D-allose inhibits Arabidopsis growth but fails to trigger growth retardation in the AtHXK1 loss-of function mutant (gin2 mutant)
malfunction
-
transgenic Solanum tuberosum roots are altered in their hexokinase activity by transformation with an hexokinase cDNA in sense or antisense orientation. Altering root hexokinase activity levels impacts on growth rate and hexokinase has a high flux control coefficient over glucose phosphorylation but does not control glycolytic flux or respiration rate. It is concluded that futile cycling of hexose-phosphate can be partially responsible for the differences in energetic status in roots with high and low hexokinase activity and possibly cause the observed alterations in growth in transgenic roots
malfunction
-
hypoxia-inducible factor (HIF)-1-regulated glycolytic enzyme hexokinase II (HKII) acts as a molecular switch that determines cellular fate by regulating both cytoprotection and induction of apoptosis based on the metabolic state. Together with phosphoprotein enriched in astrocytes (PEA15), HKII inhibits apoptosis after hypoxia. In contrast, HKII accelerates apoptosis in the absence of PEA15 and under glucose deprivation
metabolism
-
HKI exclusively promotes glycolysis; HKII promotes glycolysis when bound to mitochondria. Promotes glycogen synthesis when located in the cytosol
physiological function
-
glucokinase regulates glucose storage and disposal in the liver, altered glucokinase regulation in liver enhances glycolytic flux, promoting hepatic glucose metabolism and elevating concentrations of malonyl-CoA, a substrate for de novo lipogenesis
physiological function
-
glucokinase is a key regulatory enzyme in the pancreatic beta-cell, it plays a crucial role in the regulation of insulin secretion and has been termed the glucose sensor in pancreatic beta-cells
physiological function
-
overexpressed glucokinase due to its structural similarity with Mlc, the repressor of malT, binds to the glucose transporter (PtsG), releasing Mlc and thus increasing malT repression
physiological function
Trichosporonoides megachiliensis
-
part of pentose phosphate pathway
physiological function
-
glucokinase acts as a hepatic glucose sensor that permits hepatic metabolism to respond appropriately to changes in plasma glucose concentrations
physiological function
-
pHXK is a node of convergence for sugar-mediated and plastid gene expression (PGE)-derived signals in Arabidopsis thaliana
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-dATP + D-glucose
2'-dADP + D-glucose 6-phosphate
show the reaction diagram
-
73% of the activity with ATP
-
-
?
2'-dATP + D-glucose
2'-dADP + D-glucose 6-phosphate
show the reaction diagram
-
73-80% of the activity with ATP, isoenzyme Hex A, B, C
-
-
?
2'-dATP + D-glucose
2'-dADP + D-glucose 6-phosphate
show the reaction diagram
-
Hex A: 73% of the activity with ATP, Hex B: 76% of the activity with ATP, Hex C: 80% of the activity with ATP
-
-
?
2-fluoro-2-deoxy-D-glucose + ATP
2-fluoro-2-deoxy-D-glucose 6-phosphate + ADP
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 + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
Q95PL2
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
Q7ZAH1, -
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
Q96Y14, -
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
30% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
Hex Ia: 95% of the activity with glucose, Hex Ib: 99% of the activity with glucose, Hex Ic: 74% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
hexokinase Ia: 65% of the activity with glucose, hexokinase Ib: 70% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
hexokinase III: 151% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
54% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
Hex A: 93% of the activity with glucose, Hex B: 51% of the activity with glucose, Hex C: 48% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
93% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
65.7% of the activity with glucose, erythrocyte enzyme
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
hexokinase I: as effective as glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-
84% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
-, Q96VP5
17% of activity with D-fructose at 50 mM substrate concentration
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
Q5RLG0, -
42% of the activity with D-glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
Sulfolobus tokodaii 7
Q96Y14
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
Thermus caldophilus GK24
Q5RLG0
42% of the activity with D-glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
show the reaction diagram
Drosophila melanogaster Samarkand
-
Hex A: 93% of the activity with glucose, Hex B: 51% of the activity with glucose, Hex C: 48% of the activity with glucose
-
-
?
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-allose
ADP + D-allose 6-phosphate
show the reaction diagram
Q5RLG0, -
58% of the activity with D-glucose
-
-
?
ATP + D-allose
ADP + D-allose 6-phosphate
show the reaction diagram
-
phosphorylation of D-allose at C6 by hexokinase is essential since it up-regulates expression of transcription factor OsABF1
-
-
?
ATP + D-allose
ADP + D-allose 6-phosphate
show the reaction diagram
Thermus caldophilus GK24
Q5RLG0
58% of the activity with D-glucose
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
P04807
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
-, Q6Q8A5
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
Q3S2I3, -
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
P04806
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
A1Z0M7, -
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
-, Q56VN6
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
B8K2W7, -
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
Q5SLJ4, -
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
Q96Y14, -
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
-, Q96VP5
best substrate
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
Q5RLG0, -
16% of the activity with D-glucose
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
-
isozyme HKI, isozyme HKII is highly specific for D-fructose
-
-
?
ATP + D-fructose
?
show the reaction diagram
A0SZU9
-
-
-
?
ATP + D-galactose
ADP + D-galactose 6-phosphate
show the reaction diagram
Q5SLJ4, -
-
-
-
?
ATP + D-galactose
?
show the reaction diagram
-, Q56VN6
-
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
show the reaction diagram
Q96Y14, -
-
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
show the reaction diagram
Q5RLG0, -
67% of the activity with D-glucose
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
show the reaction diagram
-, Q96VP5
8% of activity with D-fructose at 50 mM substrate concentration
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
show the reaction diagram
Thermus caldophilus GK24
Q5RLG0
67% of the activity with D-glucose
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
P19367
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
P04807
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
O64390, Q9SQ76, -
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Q95PL2
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
P33284
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-, Q6Q8A5
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Q5W5U3
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Q3S2I3, -
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
A0SZU9
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
P04806
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
A1Z0M7, -
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-, Q56VN6
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
P35557
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
B8K2W7, -
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Q5SLJ4, -
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Q96Y14, -
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Q5RLG0, -
best substrate
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-, Q96VP5
enzyme mediates glucose repression
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
first step in glucose metabolism, pathway overview, isozyme types are differently regulated and catalytically active, isozyme type I is involved in catabolism, while type II and III are involved in anabolism, the activity rate of type I isozyme i correlated with the oxidative phosphorylation rate, overview
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
first step in the process of glycolysis
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Q5W5U3
involved in glucose catabolism
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-, Q6Q8A5
isozyme hexokinase 2 plays a role in starch and secondary metabolism in starch sheath, xylem parenchyma, guard cells, and root tips
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-, Q96VP5
39% of activity with D-fructose at 50 mM substrate concentration
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
isozyme HKI
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
control of GK activity and Km through the ratio of distinct conformers (super-open, open, and closed) through either substrate or other ligand binding and/or dissociation
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
the presence of 0.5 mM glucose induced total hexokinase activity in supernatants from sperm extracts of 1.7 mIU/mg protein, while the same concentration of both fructose, mannose, and sorbitol induced total hexokinase activity from 0.3 mIU/mg protein to 0.60 IU/mg protein. Diluted boar sperm from fresh ejaculates phosphorylates glucose through the hexokinase step much more efficiently than fructose or mannose. This difference facilitates a much more rapid intake of glucose into glycolysis than the other sugars
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
hexokinase II displays high affinity for D-glucose
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
under physiological conditions D-glucose is the preferred substrate
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Q96Y14, -
in Sulfolobus tokodaii this is the sole enzyme responsible for the phosphorylation of glucose in vivo
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Sulfolobus tokodaii 7
Q96Y14
-, in Sulfolobus tokodaii this is the sole enzyme responsible for the phosphorylation of glucose in vivo
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Thermus caldophilus GK24
Q5RLG0
best substrate
-
-
?
ATP + D-maltose
?
show the reaction diagram
-, Q56VN6
-
-
-
?
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
-
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
-, Q6Q8A5
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
Q3S2I3, -
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
-, Q56VN6
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
B8K2W7, -
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
Q5SLJ4, -
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
Q96Y14, -
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
-, Q96VP5
33% of activity with D-fructose at 50 mM substrate concentration
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
Q5RLG0, -
75% of the activity with D-glucose
-
-
?
ATP + D-mannose
?
show the reaction diagram
A0SZU9
-
-
-
?
ATP + hexose
ADP + hexose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
Q96Y14, -
-
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
Q3S2I3, -
-
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
B8K2W7, -
-
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
-
MgCTP, hexokinase I: 5% of the activity with ATP
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
-
11% of the activity with ATP, isoenzyme Hex C, not: isoenzyme Hex A and Hex B
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
-
35% of the activity with ATP
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
-
35% of the activity with ATP
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
-
Hex B: 5% of the activity with ATP, Hex C: 11% of the activity with ATP, not Hex A
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
Q96Y14, -
81% of the activity with ATP
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
show the reaction diagram
Catharanthus roseus B/TH
-
35% of the activity with ATP
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
Q95PL2
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
Q7ZAH1, -
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
poor substrate
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
hexokinase C
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
46.3% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
HK3: 16% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
hexokinase III: 12.6% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
hexokinase I: 130% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
70% of the activity with glucose, erythrocyte enzyme
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
Q969A8, -
79% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
hexokinase Ia: 69% of the activity with glucose, hexokinase Ib: 42% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
hexokinase, but not glucokinase
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
HK1: 4% of the activity with glucose, HK2: 3% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
P50521, Q09756
higher activity than with glucose or mannose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
Hex Ia: 100% of the activity with glucose, Hex Ib: 120% of the activity with glucose, Hex Ic: 90% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
hexokinases PI and PII phosphorylate fructose 2.5 and 1.5times faster than glucose, glucokinase: very low or no activity
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
110% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
Hex A: 50% of the activity with glucose, Hex B: 41% of the activity with glucose, Hex C: 134% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
50% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
-
HK3: 5% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
Catharanthus roseus B/TH
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
Schizosaccharomyces pombe PB003
Q09756
higher activity than with glucose or mannose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
Saccharomyces cerevisiae G-517
-
hexokinases PI and PII phosphorylate fructose 2.5 and 1.5times faster than glucose, glucokinase: very low or no activity
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
Drosophila melanogaster Samarkand
-
Hex A: 50% of the activity with glucose, Hex B: 41% of the activity with glucose, Hex C: 134% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
Drosophila melanogaster Samarkand
-
50% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
show the reaction diagram
Schizosaccharomyces pombe PB004
P50521
higher activity than with glucose or mannose
-
-
?
D-fructose + ATP
D-fructose 6-phosphate + ADP
show the reaction diagram
-
-
-
-
?
D-fructose + ATP
D-fructose 6-phosphate + ADP
show the reaction diagram
-
fructose metabolism
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
-
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
show the reaction diagram
Q95PL2
-
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
show the reaction diagram
-
Hex A: 19% of the activity with glucose, Hex C: 44% of the activity with glucose, not Hex B
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
show the reaction diagram
-
Hex Ia and Ib: 47% of the activity with glucose, Hex Ic: 21% of the activity with glucose
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
show the reaction diagram
-
hexokinase III: 35% of the activity with glucose
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
show the reaction diagram
-
44.9% of the activity with glucose
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
show the reaction diagram
-
hexokinase Ia: 35% of the activity with glucose, hexokinase Ib: 70% of the activity with glucose
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
show the reaction diagram
-
erythrocyte enzyme, 43.4% of the activity with glucose
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
show the reaction diagram
-
hexokinase I: 40% of the activity with glucose
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
show the reaction diagram
Drosophila melanogaster Samarkand
-
Hex A: 19% of the activity with glucose, Hex C: 44% of the activity with glucose, not Hex B
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
P19367
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
P05708
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
specific for ATP
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
Q969A8, -
specific for ATP
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
good substrate
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
good substrate
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
P50521, Q09756
11% of the activity with fructose
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
Q8ST54
specific for glucose
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
bound glucose is present as the beta-anomer, glucose binding sites
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
P50521, Q09756
59% of the activity with fructose
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
Q7ZAH1, -
preferred specificity for glucose
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
Q969A8, -
preferred specificity for glucose
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
hexokinase and glucokinase
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
absolute requirement for D-glucose
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
the binding of glucose does not depend on ATP, and vice versa
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
most active with D-glucose
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
MgATP2-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
MgATP2-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
MgATP2-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
MgATP2-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
-
hexokinase bound at type A and B sites of brain mitochondria selectively uses intramitochondrial ATP as substrate, but hexokinase bound at type B sites, after removal of enzyme of type A sites, shows no such selectivity
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
Catharanthus roseus B/TH
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
Schizosaccharomyces pombe NCYC 132S2-2
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
Schizosaccharomyces pombe PB003
Q09756
11% of the activity with fructose
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
Saccharomyces cerevisiae G-517
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
Drosophila melanogaster Samarkand
-
the binding of glucose does not depend on ATP, and vice versa
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
Drosophila melanogaster Samarkand
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
Schizosaccharomyces pombe PB004
P50521
59% of the activity with fructose
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
show the reaction diagram
Entamoeba histolytica SFL-3
-
good substrate
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glycolytic enzyme
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glycolytic enzyme
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glycolytic enzyme
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
Q8ST54
glycolytic enzyme
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
key enzyme in the control of brain glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
cerebral glycolytic metabolism, mechanisms for regulation of mitochondrial hexokinase activity may depend on the ratio of type A:type B sites
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
P19367
hexokinase I governs the rate-limiting step of glycolysis in brain
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
binding of brain enzyme to the outer mitochondrial membrane plays a role in regulation of hexokinase activity in vivo, and thereby of the cerebral glycolytic rate
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
Q969A8, -
first step of the glycolytic pathway, physiological function of membrane-bound hexokinase in the tachyzoite: glucose channeling with a glucose/hexose transporter
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
enzyme of the glucose-phosphate branch of the oxidative pentose phosphate pathway
-
?
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-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
hexokinase I is the pacemaker of glycolysis in brain tissue
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
hexokinase I is a regulated enzyme and serves a critical role in controlling the rate of glycolysis in both brain and red blood cells
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
organ- and development-specific changes in the abundance of the various enzyme forms contribute to the regulation of hexose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
rate-limiting step in the glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
Q969A8, -
rate-limiting step in the glycolysis
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
the presence of type III hexokinase enables the adult pig erythrocytes to metabolize low but appreciable amounts of glucose
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
Q7ZAH1, -
carbohydrate metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
initial catalytic step of the cerebral glucose metabolism, glucose 6-phosphate represents a major regulatory influence on the in vivo activity
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
initial enzyme of glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
initial enzyme of glycolysis, at high energy charge HXK1 may be involved in glycolysis and in some biosynthetic processes, e.g. phosphorylating mannose or glucose for the later integration into membrane components, at low energy charge HXK1 could be inhibited by AMP and ADP, and HXK2 would be more active and could keep up glucokinase activity for glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
isoenzymes are a target for effective control of glucose 6-phosphate formation by energy charge of the cell or by the intracellular level of ATP, ADP and glucose instead of allosteric interconversions of the enzyme
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
Schizosaccharomyces pombe NCYC 132S2-2
-
enzyme of the glucose-phosphate branch of the oxidative pentose phosphate pathway
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
Entamoeba histolytica SFL-3
-
initial enzyme of glycolysis
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
Q95PL2
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
Q7ZAH1, -
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
good substrate
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
Hex Ia: 78% of the activity with glucose, Hex Ib: 83% of the activity with glucose, Hex Ic: 85% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
hexokinase I: 106% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
hexokinase III: 85% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
HXK1: good substrate, HXK2: much lower phosphorylation rate than of HXK1
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
82% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
Q969A8, -
55% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
P50521, Q09756
42% of the activity with fructose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
109% of the activity with glucose, erythrocyte enzyme
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
P50521, Q09756
23% of the activity with fructose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
104-105% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
27.2% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
Hex A: 100% of the activity with glucose, Hex B: 98% of the activity with glucose, Hex C: 44% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
glucokinase
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
-
HK1: 53% of the activity with glucose, HK2: 22% of the activity with glucose, HK3: 45% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
Schizosaccharomyces pombe PB003
Q09756
23% of the activity with fructose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
Saccharomyces cerevisiae G-517
-
glucokinase
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
Drosophila melanogaster Samarkand
-
Hex A: 100% of the activity with glucose, Hex B: 98% of the activity with glucose, Hex C: 44% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
Schizosaccharomyces pombe PB004
P50521
42% of the activity with fructose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
show the reaction diagram
Entamoeba histolytica SFL-3
-
HXK1: good substrate, HXK2: much lower phosphorylation rate than of HXK1
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
show the reaction diagram
Q3S2I3, -
-
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
show the reaction diagram
B8K2W7, -
-
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
show the reaction diagram
Q96Y14, -
52% of the activity with ATP
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
show the reaction diagram
-
can partially replace ATP
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
show the reaction diagram
Q7ZAH1, -
18% of the activity with ATP
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
show the reaction diagram
Catharanthus roseus, Catharanthus roseus B/TH
-
19% of the activity with ATP
-
-
?
hexose + ATP
ADP + hexose 6-phosphate
show the reaction diagram
-
-
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
show the reaction diagram
-
30% of the activity with ATP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
show the reaction diagram
Q7ZAH1, -
40% of the activity with ATP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
show the reaction diagram
-
12% of the activity with ATP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
show the reaction diagram
-
hexokinase III: 24% of the activity with glucose
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
show the reaction diagram
-
13.5-14% of the activity with ATP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
show the reaction diagram
-
36% of the activity with ATP, erythrocyte enzyme
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
show the reaction diagram
-
MgITP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
show the reaction diagram
-
MgITP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
show the reaction diagram
-
MgITP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
show the reaction diagram
-
hexokinase I: 9% of the activity with ATP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
show the reaction diagram
Q96Y14, -
64% of the activity with ATP
-
-
?
N-acetyl-D-glucosamine + ATP
ADP + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
erythrocyte enzyme, 32.6% of the activity with glucose
-
-
?
TTP + D-glucose
TDP + D-glucose 6-phosphate
show the reaction diagram
Q3S2I3, -
-
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
Q3S2I3, -
-
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
B8K2W7, -
-
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
Q7ZAH1, -
17% of the activity with ATP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
-
14% of the activity with ATP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
Q96Y14, -
37% of the activity with ATP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
-
can partially replace ATP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
-
23% of the activity with ATP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
-
hexokinase I: 5% of the activity with ATP, MgUTP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
-
MgUTP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
show the reaction diagram
Catharanthus roseus B/TH
-
23% of the activity with ATP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
show the reaction diagram
Sulfolobus tokodaii 7
Q96Y14
64% of the activity with ATP
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
Q7ZAH1, -
not: ADP
-
-
-
additional information
?
-
Q969A8, -
not: ADP
-
-
-
additional information
?
-
-
ligand binding sites in the N- and C-terminal halves and interactions between these sites
-
-
-
additional information
?
-
-
not: UTP
-
-
-
additional information
?
-
-
not: UTP
-
-
-
additional information
?
-
-
not: UTP
-
-
-
additional information
?
-
-
not: UTP
-
-
-
additional information
?
-
-
not: UTP
-
-
-
additional information
?
-
-
not: UTP
-
-
-
additional information
?
-
Q969A8, -
not: UTP
-
-
-
additional information
?
-
-
structure model of hexokinase I
-
-
-
additional information
?
-
P19367
structure model of hexokinase I
-
-
-
additional information
?
-
P05708
structure model of hexokinase I
-
-
-
additional information
?
-
Q7ZAH1, -
not: ribose, xylose, phosphorylated hexoses, UDP, polyphosphates
-
-
-
additional information
?
-
Q969A8, -
not: diphosphate
-
-
-
additional information
?
-
Q8ST54
not: diphosphate
-
-
-
additional information
?
-
-
glucokinase: not: fructose, galactose, sorbose, rhamnose, arabinose, mannitol, sorbitol, ribose
-
-
-
additional information
?
-
-
not: N-acetyl-D-glucosamine
-
-
-
additional information
?
-
-
not: N-acetyl-D-glucosamine
-
-
-
additional information
?
-
-
not: N-acetyl-D-glucosamine
-
-
-
additional information
?
-
Q8ST54
not: mannose
-
-
-
additional information
?
-
-
not: fructose
-
-
-
additional information
?
-
Q8ST54
not: fructose
-
-
-
additional information
?
-
-
role of the hexokinase III carboxyl-domain in determining the catalytic properties of enzyme
-
-
-
additional information
?
-
-
not: D-galactose
-
-
-
additional information
?
-
-
not: D-galactose
-
-
-
additional information
?
-
-
not: D-galactose
-
-
-
additional information
?
-
-
not: D-galactose
-
-
-
additional information
?
-
-
not: D-galactose
-
-
-
additional information
?
-
-
not: D-galactose
-
-
-
additional information
?
-
-
not: D-galactose
-
-
-
additional information
?
-
Q7ZAH1, -
not: D-galactose
-
-
-
additional information
?
-
Q969A8, -
not: D-galactose
-
-
-
additional information
?
-
Q8ST54
not: D-galactose
-
-
-
additional information
?
-
-
not: ITP
-
-
-
additional information
?
-
Q969A8, -
not: ITP
-
-
-
additional information
?
-
-
not: N-acetylmannosamine, 6-deoxy-6-aminoglucose
-
-
-
additional information
?
-
P05708
allosteric regulation of hexokinase I, the functional regulatory glucose 6-phosphate binding site is located in the N-terminal half
-
-
-
additional information
?
-
-
isolated catalytically active 51 kDa C-fragment and 52 kDa N-fragment without catalytic activity, both fragments contain discrete binding sites for hexoses and hexose 6-phosphates, one of each pair of sites must be latent in the intact enzyme, the regulatory site binding glucose 6-phosphate is associated with the N-terminal half
-
-
-
additional information
?
-
-
the 50 kDa C-terminal half of HK I contains the catalytic domain, the N-terminal half is catalytically inactive
-
-
-
additional information
?
-
-
allosteric enzyme, catalyzes phosphoryl transfer from MgATP2- to the 6-OH group of a number of furanose- and pyranose-type compounds
-
-
-
additional information
?
-
-
C-terminal catalytic and N-terminal regulatory domain, detailed structure of hexokinase I, substrate binding sites, models for regulation
-
-
-
additional information
?
-
-
not: trehalose
-
-
-
additional information
?
-
-
not: GTP
-
-
-
additional information
?
-
-
not: GTP
-
-
-
additional information
?
-
-
not: GTP
-
-
-
additional information
?
-
-
not: GTP
-
-
-
additional information
?
-
-
not: GTP
-
-
-
additional information
?
-
-
not: GTP
-
-
-
additional information
?
-
Q969A8, -
not: GTP
-
-
-
additional information
?
-
-
not: CTP
-
-
-
additional information
?
-
-
not: CTP
-
-
-
additional information
?
-
-
not: CTP
-
-
-
additional information
?
-
-
not: CTP
-
-
-
additional information
?
-
Q7ZAH1, -
not: CTP
-
-
-
additional information
?
-
Q969A8, -
not: CTP
-
-
-
additional information
?
-
-
sperm hexokinase p95/116 may serve as cell surface receptor kinase for the zona pellucida glycoprotein ZP3
-
-
-
additional information
?
-
-
hexokinase PI is a constitutive enzyme, hexokinase PII and glucokinase are regulated by the carbon source used
-
-
-
additional information
?
-
-
the 100 kDa isozymes, displaying internal sequence repetition, may have evolved by gene duplication of a 50 kDa ancestor
-
-
-
additional information
?
-
P33284
the enzyme is the only glucose and fructose phosphorylating enzyme, which is upregulating glucose transport and also mediating glucose repression
-
-
-
additional information
?
-
Q5RLG0, -
no activity with D-galactose and N-acetylglucosamine, enzyme shows broad substrate specificity, specificity probably depends on the interaction energy occurring by the positional proximity of sugars bound in the active site
-
-
-
additional information
?
-
-, Q96VP5
no activity with D-xylose, D-galactose, and methyl-alpha-D-glucoside
-
-
-
additional information
?
-
-
relatively nonspecific enzyme
-
-
-
additional information
?
-
Q5W5U3
the active site is located in the C-terminal domain
-
-
-
additional information
?
-
-
glucokinase regulates reproductive function, glucocorticoid secretion, food intake, and hypothalamic gene expression
-
-
-
additional information
?
-
P05708, P27881
hexokinase I and hexokinase II are independently regulated, implying that they perform different roles in cardiac glucose regulation
-
-
-
additional information
?
-
A1Z0M7, -
hexokinase, Hxk1, but not the glucokinase, Glk1, is required for normal growth and sugar metabolism, and for pathogenicity on fruits
-
-
-
additional information
?
-
-, Q2KNB5, Q2KNB9, Q5W676, Q6Z398, Q8LH82
OsHXK2 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
-
additional information
?
-
-, Q2KNB5, Q2KNB9, Q5W676, Q6Z398, Q8LH82
OsHXK5 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
-
additional information
?
-
-, Q2KNB5, Q2KNB9, Q5W676, Q6Z398, Q8LH82
OsHXK6 expression appeared to be significantly upregulated in rice leaves by glucose and fructose
-
-
-
additional information
?
-
-, Q2KNB5, Q2KNB9, Q5W676, Q6Z398, Q8LH82
OsHXK8 may function in the endosperm in the filling phase of rice seed development
-
-
-
additional information
?
-
-
role of a bound glucokinase protein fraction in the regulation of insulin granule movement along tubulin filaments
-
-
-
additional information
?
-
-
the enzyme plays a role in glycogen synthesis and glucose homeostasis
-
-
-
additional information
?
-
Q95PL2
the C-terminal tail of TbHK1 is important for hexokinase activity
-
-
-
additional information
?
-
-
G/F discrepancy in Saccharomyces cerevisiae is not related to the maximal hexokinase activity in vitro with glucose or fructose as substrate or to the ratio between the Km values for glucose and fructose phosphorylation but might rather be related to the actual fructose phosphorylating activity at physiological fructose levels in vivo
-
-
-
additional information
?
-
Q96Y14, -
galactose is phosphorylated at rates of 0.8 and 0.08 U/mg at concentrations of 1 and 10 mM, respectively. Ribose, xylose, N-acetylmannosamine, glucose-1-phosphate, and fructose-6-phosphate (10 mM) are not phosphorylated by the enzyme
-
-
-
additional information
?
-
Q969A8
not: ADP, not: UTP, not: diphosphate, not: D-galactose, not: ITP
-
-
-
additional information
?
-
Sulfolobus tokodaii 7
Q96Y14
galactose is phosphorylated at rates of 0.8 and 0.08 U/mg at concentrations of 1 and 10 mM, respectively. Ribose, xylose, N-acetylmannosamine, glucose-1-phosphate, and fructose-6-phosphate (10 mM) are not phosphorylated by the enzyme
-
-
-
additional information
?
-
Thermus caldophilus GK24
Q5RLG0
no activity with D-galactose and N-acetylglucosamine, enzyme shows broad substrate specificity, specificity probably depends on the interaction energy occurring by the positional proximity of sugars bound in the active site
-
-
-
additional information
?
-
Saccharomyces cerevisiae G-517
-
glucokinase: not: fructose, galactose, sorbose, rhamnose, arabinose, mannitol, sorbitol, ribose, hexokinase PI is a constitutive enzyme, hexokinase PII and glucokinase are regulated by the carbon source used
-
-
-
additional information
?
-
Entamoeba histolytica SFL-3
-
not: fructose, not: D-galactose
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
P04807
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
Q6Q8A5
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
P04807
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
P33284
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-, Q96VP5
enzyme mediates glucose repression
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
first step in glucose metabolism, pathway overview, isozyme types are differently regulated and catalytically active, isozyme type I is involved in catabolism, while type II and III are involved in anabolism, the activity rate of type I isozyme i correlated with the oxidative phosphorylation rate, overview
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
first step in the process of glycolysis
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Q5W5U3
involved in glucose catabolism
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-, Q6Q8A5
isozyme hexokinase 2 plays a role in starch and secondary metabolism in starch sheath, xylem parenchyma, guard cells, and root tips
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
control of GK activity and Km through the ratio of distinct conformers (super-open, open, and closed) through either substrate or other ligand binding and/or dissociation
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
-
the presence of 0.5 mM glucose induced total hexokinase activity in supernatants from sperm extracts of 1.7 mIU/mg protein, while the same concentration of both fructose, mannose, and sorbitol induced total hexokinase activity from 0.3 mIU/mg protein to 0.60 IU/mg protein. Diluted boar sperm from fresh ejaculates phosphorylates glucose through the hexokinase step much more efficiently than fructose or mannose. This difference facilitates a much more rapid intake of glucose into glycolysis than the other sugars
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Q96Y14, -
in Sulfolobus tokodaii this is the sole enzyme responsible for the phosphorylation of glucose in vivo
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
Sulfolobus tokodaii 7
Q96Y14
in Sulfolobus tokodaii this is the sole enzyme responsible for the phosphorylation of glucose in vivo
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
show the reaction diagram
-, Q6Q8A5
-
-
-
?
ATP + hexose
ADP + hexose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-fructose + ATP
D-fructose 6-phosphate + ADP
show the reaction diagram
-
fructose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glycolytic enzyme
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glycolytic enzyme
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glycolytic enzyme
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
Q8ST54
glycolytic enzyme
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
key enzyme in the control of brain glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
cerebral glycolytic metabolism, mechanisms for regulation of mitochondrial hexokinase activity may depend on the ratio of type A:type B sites
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
P19367
hexokinase I governs the rate-limiting step of glycolysis in brain
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
binding of brain enzyme to the outer mitochondrial membrane plays a role in regulation of hexokinase activity in vivo, and thereby of the cerebral glycolytic rate
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
Q969A8, -
first step of the glycolytic pathway, physiological function of membrane-bound hexokinase in the tachyzoite: glucose channeling with a glucose/hexose transporter
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
enzyme of the glucose-phosphate branch of the oxidative pentose phosphate pathway
-
?
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-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
hexokinase I is the pacemaker of glycolysis in brain tissue
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
hexokinase I is a regulated enzyme and serves a critical role in controlling the rate of glycolysis in both brain and red blood cells
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
organ- and development-specific changes in the abundance of the various enzyme forms contribute to the regulation of hexose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
rate-limiting step in the glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
Q969A8, -
rate-limiting step in the glycolysis
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
the presence of type III hexokinase enables the adult pig erythrocytes to metabolize low but appreciable amounts of glucose
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
Q7ZAH1, -
carbohydrate metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
initial catalytic step of the cerebral glucose metabolism, glucose 6-phosphate represents a major regulatory influence on the in vivo activity
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
initial enzyme of glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
initial enzyme of glycolysis, at high energy charge HXK1 may be involved in glycolysis and in some biosynthetic processes, e.g. phosphorylating mannose or glucose for the later integration into membrane components, at low energy charge HXK1 could be inhibited by AMP and ADP, and HXK2 would be more active and could keep up glucokinase activity for glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
-
isoenzymes are a target for effective control of glucose 6-phosphate formation by energy charge of the cell or by the intracellular level of ATP, ADP and glucose instead of allosteric interconversions of the enzyme
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
Schizosaccharomyces pombe NCYC 132S2-2
-
enzyme of the glucose-phosphate branch of the oxidative pentose phosphate pathway
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
show the reaction diagram
Entamoeba histolytica SFL-3
-
initial enzyme of glycolysis
-
-
?
additional information
?
-
-
sperm hexokinase p95/116 may serve as cell surface receptor kinase for the zona pellucida glycoprotein ZP3
-
-
-
additional information
?
-
-
hexokinase PI is a constitutive enzyme, hexokinase PII and glucokinase are regulated by the carbon source used
-
-
-
additional information
?
-
-
the 100 kDa isozymes, displaying internal sequence repetition, may have evolved by gene duplication of a 50 kDa ancestor
-
-
-
additional information
?
-
P33284
the enzyme is the only glucose and fructose phosphorylating enzyme, which is upregulating glucose transport and also mediating glucose repression
-
-
-
additional information
?
-
-
glucokinase regulates reproductive function, glucocorticoid secretion, food intake, and hypothalamic gene expression
-
-
-
additional information
?
-
P05708, P27881
hexokinase I and hexokinase II are independently regulated, implying that they perform different roles in cardiac glucose regulation
-
-
-
additional information
?
-
A1Z0M7, -
hexokinase, Hxk1, but not the glucokinase, Glk1, is required for normal growth and sugar metabolism, and for pathogenicity on fruits
-
-
-
additional information
?
-
-, Q2KNB5, Q2KNB9, Q5W676, Q6Z398, Q8LH82
OsHXK2 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
-
additional information
?
-
-, Q2KNB5, Q2KNB9, Q5W676, Q6Z398, Q8LH82
OsHXK5 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
-
additional information
?
-
-, Q2KNB5, Q2KNB9, Q5W676, Q6Z398, Q8LH82
OsHXK6 expression appeared to be significantly upregulated in rice leaves by glucose and fructose
-
-
-
additional information
?
-
-, Q2KNB5, Q2KNB9, Q5W676, Q6Z398, Q8LH82
OsHXK8 may function in the endosperm in the filling phase of rice seed development
-
-
-
additional information
?
-
-
role of a bound glucokinase protein fraction in the regulation of insulin granule movement along tubulin filaments
-
-
-
additional information
?
-
-
the enzyme plays a role in glycogen synthesis and glucose homeostasis
-
-
-
additional information
?
-
-
G/F discrepancy in Saccharomyces cerevisiae is not related to the maximal hexokinase activity in vitro with glucose or fructose as substrate or to the ratio between the Km values for glucose and fructose phosphorylation but might rather be related to the actual fructose phosphorylating activity at physiological fructose levels in vivo
-
-
-
additional information
?
-
Saccharomyces cerevisiae G-517
-
hexokinase PI is a constitutive enzyme, hexokinase PII and glucokinase are regulated by the carbon source used
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
AMP
-
much less stimulation than by cAMP
ATP
-
absolute requirement for Mg2+ and ATP
ATP
-
requirement
ATP
-
affinity for ATP depends on the presence of a divalent metal ion, Mg2+ or Mn2+
ATP
-
absolute requirement for MgATP2-
ATP
-
activates, ATP-dependent enzyme
ATP
Q5RLG0, -
construction of a model of the enzyme-ATP/Mg2+-sugar-binding complex structure
ATP
-
formation of MgATP2- before reaction
ATP
Q5W5U3
MgATP2-
ATP
-
preferred by both isozymes HKI and HKII
cAMP
-
stimulates, 0.2-0.8 mM: 2fold
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
Q5RLG0, -
79% of the activity with Mg2+
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
Mg2+
-
activation is associated with an increase in the maximal velocity by its interaction with the ternary complex to facilitate the transfer of the phosphoryl group; maximal activity at 1 mM Mg2+, can be partially replaced by Mn2+; strict requirement for divalent metal ions
Mg2+
-
absolute requirement for Mg2+ and ATP
Mg2+
-
required
Mg2+
-
required
Mg2+
-
below 3 mM; required
Mg2+
-
Mg2+ or Mn2+ required
Mg2+
-
Mg2+-dependent
Mg2+
-
required
Mg2+
-
affinity for ATP depends on the presence of a divalent metal ion, Mg2+ or Mn2+
Mg2+
-
absolute requirement for MgATP2- and Mg2+
Mg2+
Q7ZAH1, -
strict requirement for divalent metal ions
Mg2+
Q8ST54
MgCl2 is most effective, followed by MnCl2 with 16% of the activity found with MgCl2; strict requirement for divalent metal ions
Mg2+
-
required
Mg2+
Q5RLG0, -
divalent metal ions are essential for activity, most effective metal ion, construction of a model of the enzyme-ATP/Mg2+-sugar-binding complex structure
Mg2+
-, Q96VP5
-
Mg2+
-
-
Mg2+
Q5W5U3
MgATP2-
Mg2+
-
absolutely required for activity by both isozymes HKI and HKII
Mg2+
-
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
Mg2+
-
direct visualization of the binding mode for magnesium to hexokinase
Mg2+
-
required for activity
Mn2+
-
Mg2+ or Mn2+ required
Mn2+
-
affinity for ATP depends on the presence of a divalent metal ion, Mg2+ or Mn2+
Mn2+
Q7ZAH1, -
Mg2+ can be partially replaced by Mn2+; strict requirement for divalent metal ions
Mn2+
Q8ST54
MgCl2 is most effective, followed by MnCl2 with 16% of the activity found with MgCl2; strict requirement for divalent metal ions
Mn2+
Q5RLG0, -
73% of the activity with Mg2+
Ni2+
Q5RLG0, -
92% of the activity with Mg2+
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
Q5RLG0, -
different buffers have no effect on the enzyme activity
additional information
-
no activity in the presence of Zn2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2-pyridin-4-ylethane-1,1-diyl)bis(phosphonic acid)
-
mixed to non-competitive inhibitors against ATP, non-competitive against D-glucose
(3-bromo-phenyl)-aminomethylene-1,1-bisphosphonate
-
-
(9-ethyl-9H-3-carbazolyl)-aminomethylene-1,1-bisphosphonate
-
-
1,10-phenanthroline
-, Q56VN6
20 mM, 96% inhibition
1,5-Anhydro-D-glucitol 6-phosphate
-
HK I and HK I+, the D84A mutant of HK I has 2fold increased Ki, HK I: low millimolar concentrations of phosphate antagonize inhibition by competing for an anion binding site in the N-terminal half of HK I, HK I+: insert abolishes the antagonism of phosphate
1,5-Anhydro-D-glucitol 6-phosphate
-
intact enzyme and catalytically active 51 kDa C fragment of hexokinase
1,5-Anhydro-D-glucitol 6-phosphate
-
less effective than glucose 6-phosphate, competitive versus ATP
1,5-Anhydro-D-glucitol 6-phosphate
P19367
wild-type and nonaggregating interface mutant hexokinase I, inhibition is relieved by phosphate
1,5-Anhydro-D-glucitol 6-phosphate
P05708
hexokinase I, antagonism by phosphate at low concentrations
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
1,5-Anhydro-D-glucitol 6-phosphate
-
-
1,5-anhydroglucitol-6-phosphate
-
potent inhibition of type I isozyme in absence of oxidative phosporylation and with extramitochondrial ATP, weak inhibition with ATP supplied by oxidative phosphorylation
2,3-diphosphoglycerate
-
hexokinase III
2,3-diphosphoglycerate
-
-
2-(pyridin-4-yl)-1-hydroxyethane-1,1-bisphosphonate
-
-
2-deoxy-D-glucose
P50521, Q09756
;
2-deoxy-D-glucose
-
low substrate inhibition
2-phosphoglycerate
-
hexokinase III
2-phosphoglycerate
-
-
2-Phosphoglycerol
-
-
3-bromo-2-oxopropionic acid
-
-
3-Bromopyruvate
-
in mice treated with 3-bromopyruvate, mean tumor volumes and tumor volume growth are significantly reduced
3-phosphoglycerate
-
hexokinase III
3-phosphoglycerate
-
-
5,5'-dithiobis-(2-nitrobenzoic acid)
-
inactivation, protection by MgADP-, AMP, 2-deoxyglucose, glucose, and mannose probably via binary complex formation, no protection by glucose 6-phosphate, slight protection by MgATP2-
5-thio-D-glucose
-
marked inhibition
5-thio-D-glucose
-
-
6-deoxy-D-glucose
-
-
acetate
-
noncompetitive to glucose
acidic phospholipids
-
irreversible inhibition, binds at the nucleotide-binding site of enzyme, ATP and glucose 6-phosphate protect, effectiveness of various ligands in protection against inhibition, effect of pH and temperature
-
adenosine
-
at 10 mM, recombinant HXK1: 36% inhibition, recombinant HXK2: 5% inhibition
ADP
-
noncompetitive to glucose, competitive to ATP
ADP
-
noncompetitive to glucose, competitive to ATP
ADP
-
4 mM: 50% inhibition
ADP
-
isoenzymes HK1 and HK2, competitive to ATP, 0.5 mM: 4-5fold inhibition
ADP
-
hexokinase III
ADP
-
mixed inhibitor versus both MgATP2- and glucose
ADP
Q8ST54
natural hexokinase from epimastigotes
ADP
-
strong, recombinant HXK1 and 2, HXK1 is more sensitive to inhibition than HXK2
ADP
-
competitive versus ATP, inhibition mode, 91.3% decreased activity
ADP
-
competitive versus ATP, both isozymes HKI and HKII
ADP
-
1 mM, 92% inhibition. Competitive inhibition versus ATP, noncompetitive inhibition versus D-glucose
ADP
-
0.1 mM, 60% inhibition
ADP
-
1 mM, 50% inhibition; about 50% inhibition at 1 mM
ADP
-
0.1 mM, 60% inhibition
ADP
-
5 mM, about 50% inhibition
ADP
O64390, Q9SQ76
hexokinase 1
ADP
-
1 mM, 45% inhibition, enzyme from kernel. Inhibits non-cytosolic enzyme from root. No inhibition of the cytosolic enzyme from root; inhibition of non-cytosolic enzyme, no inhibition of cytosolic enzyme
ADP
Q3S2I3, -
0.5 mM, 43% inhibition
ADP
-, Q56VN6
0.0001 mM, 50% inhibition. Noncompetitive inhibition with the substrate glucose
Alloxan
-
alloxan treatment (100 mg/kg) leads to an 81% reduction in glucokinase immunoreactivity and a greater than 90% reduction in glucokinase enzymatic activity in the liver
AMP
-
strong, recombinant HXK1 and 2, HXK1 is more sensitive to inhibition than HXK2
AMP
-
binds to free enzyme and to D-glucose-enzyme
AMP
-
51.4% decreased activity
AMP
-
competitive versus ATP, both isozymes HKI and HKII
AMP
-
1 mM, 73% inhibition
arsenate
-
catalytically active 51 kDa C fragment of hexokinase
ATP
-
uncomplexed, competitive to MgATP2-, erythrocyte enzyme
ATP
-
isoenzymes PII and PIIM are strongly inhibited by high physiological concentrations, 5 mM: 50% inhibition
ATP
-
ATP4-; hexokinase III; uncomplexed, competitive to MgATP2-, erythrocyte enzyme
ATP
-
ATP4-; potent inhibitor of mitochondrial HK I
ATP
-
uncomplexed, competitive to MgATP2-, erythrocyte enzyme
Br-
-
noncompetitive to glucose
CaCl2
-, Q56VN6
10 mM, 98% inhibition
cardiolipin
-
effectiveness of various ligands in protection against inhibition, effect of pH and temperature
CDP
-
1 mM, 33% inhibition
Cibacron blue
-
competitive to ATP
citrate
-
noncompetitive to glucose and ATP
Cl-
-
noncompetitive to glucose
Cl-
-
reversible, 0.25 M NaCl or KCl: 50% inhibition, at a comparable concentration of LiCl: 30% inhibition
CoA
-
54.1% decreased activity
Cr(III)-ATP
-
complex of ATP with chromium in the 3+ oxidation state, mixed versus MgATP2-, competitive inhibition versus 2-deoxyglucose
D-fructose 1,6-diphosphate
-
hexokinase III
D-fructose 1,6-diphosphate
-
-
D-fructose 6-phosphate
-
hexokinase III
D-fructose 6-phosphate
-
-
D-fructose 6-phosphate
-
product inhibition, both isozymes HKI and HKII
D-fructose 6-phosphate
-
10 mM, 33% inhibition
D-glucosamine
P50521, Q09756
;
D-glucosamine
Q3S2I3, -
20 mM, 67% inhibition
D-glucosamine
-, Q56VN6
-
D-glucose
-
hexokinase C: above 0.2 mM, inhibition partially relieved by ATP concentrations above 1 mM, inhibition is not pH-dependent
D-glucose
-
higher than 0.4 mM; inhibits hexokinase III
D-glucose
-
at high concentrations; inhibits hexokinase III
D-glucose
-
higher than 100 mM; inhibits hexokinase III
D-glucose
-
hexokinase type III, but not its catalytically active recombinant carboxyl-domain, at concentrations above 0.5 mM
D-glucose
-
substrate inhibition of type III isozyme above 1 mM, antagonized by ATP
D-Glucose 1,6-bisphosphate
Q5W5U3
competitive versus MgATP2-, low concentration of phosphate counteract
D-glucose 1,6-diphosphate
-
-
D-glucose 1,6-diphosphate
-
competitive to MgATP2-, inhibition is partially relieved by phosphate
D-glucose 1,6-diphosphate
-
hexokinase III
D-glucose 1,6-diphosphate
-
at concentrations higher than 0.2 mM, inhibits in a concentration-dependent manner, 1.2 mM: almost complete inhibition
D-glucose 1,6-diphosphate
-
-
D-glucose 1,6-diphosphate
-
strong inhibition of a recombinant full-length HK I, a truncated form lacking the first 11 amino acids named HK-11aa, and of the 50 kDa C-terminal half containing the catalytic domain, strongly pH-dependent, inhibition is reversed by phosphate, except that of the C-terminal half
D-glucose 1,6-diphosphate
-
15.7% decreased activity
D-glucose 6-phosphate
-
linear competitive inhibition with MgATP2- as varied substrate
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
inhibition of HK I, antagonism of inhibition by low millimolar concentrations of phosphate results from competition of this ligands for an anion binding site in the N-terminal half of HK I, mechanism
D-glucose 6-phosphate
-
marked inhibition of particulate hexokinase I activity
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
hexokinase I inhibition is relieved by inorganic phosphate, but not the inhibition of hexokinase II
D-glucose 6-phosphate
-
reversible product inhibition
D-glucose 6-phosphate
-
inhibitor blocks the action of hexokinase by effecting a conformational change in the structure of enzyme
D-glucose 6-phosphate
-
competitive to MgATP2-; inhibition is partially relieved by phosphate
D-glucose 6-phosphate
-
competitive versus ATP; hexokinase C: strong inhibition
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
isoenzyme HK1, not HK2, noncompetitive to glucose
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
hexokinase III, poor inhibitor, not relieved by phosphate
D-glucose 6-phosphate
-
potent inhibitor of mitochondrial HK I
D-glucose 6-phosphate
-
potent inhibition of hexokinase I is relieved by physiological levels of phosphate, mechanism
D-glucose 6-phosphate
-
strong inhibition, potential physiological effector
D-glucose 6-phosphate
-
competitive versus ATP; moderate inhibition
D-glucose 6-phosphate
Q7ZAH1, -
-
D-glucose 6-phosphate
P19367
potent product inhibition, allosterically relieved by phosphate, wild-type hexokinase I and nondimerizing mutant
D-glucose 6-phosphate
-
hexokinase type III and its catalytically active recombinant carboxyl-domain
D-glucose 6-phosphate
-
competitive to MgATP2-; strong inhibition of a recombinant full-length HK I, a truncated form lacking the first 11 amino acids named HK-11aa, and of the 50 kDa C-terminal half containing the catalytic domain, at low concentrations, 0-3 mM, inhibition is reversed by phosphate, except that of the C-terminal half
D-glucose 6-phosphate
P05708
product inhibition of hexokinase I, antagonism by phosphate at low concentrations results from competition for a common anion binding site located in the N-terminal half
D-glucose 6-phosphate
-
noncompetitive inhibition
D-glucose 6-phosphate
-
54.3% decreased activity
D-glucose 6-phosphate
-
inhibition of all isozymes, with type I isozyme inhibition is antagonized by phosphate, while with type II and III isozymes phosphate causes additional inhibition
D-glucose 6-phosphate
Q5W5U3
competitive versus MgATP2-
D-glucose 6-phosphate
-
product inhibition, both isozymes HKI and HKII
D-glucose 6-phosphate
-
hexokinase activity is strongly inhibited by high, but physiological, concentrations of glucose 6-phosphate
D-glucose 6-phosphate
-
moderate sensitivity to inhibition. Inhibition is competitive with respect to both ATP and glucose
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
O64390, Q9SQ76
; hexokinase 1
D-glucose 6-phosphate
-
weak inhibition of enzyme from kernel. No effect on the enzyme from root; weak inhibition of enzyme from kernel, no inhibition of cytosolic and non-cytosolic enzyme from root
D-glucose 6-phosphate
-, Q56VN6
-
D-glucose 6-phosphate
-
feedback-inhibition in response to the physiologic concentration of D-glucose 6-phosphate
D-glucose 6-phosphate
-
D-glucose 6-phosphate at physiological concentrations is a potent inhibitor of hexokinase isoforms I and II but not of hexokinase type IV
D-mannoheptulose
-
competitive inhibition
D-mannoheptulose
-
-
D-mannose
-
competitive to D-glucose; glucokinase
D-mannose
-
competitive to D-glucose
D-mannose
Q3S2I3, -
10 mM, 88% loss of activity
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
dihydroxyacetonephosphate
-
hexokinase III
diphosphate
Q7ZAH1, -
1 mM, 70% inhibition
diphosphate
Q8ST54
natural hexokinase from epimastigotes, mixed-type inhibition
diphosphate
-
10 mM, 54% inhibition
diphosphate
-
non-competitive inhibition towards ATP, mixed-type towards D-glucose; non-competitive inhibitor
diphosphate
-, Q56VN6
mixed type of inhibition when ATP is used as substrate
EDTA
Q7ZAH1, -
2.5 mM, complete inhibition
EDTA
-, Q56VN6
40 mM, 91% inhibition
F-
-
noncompetitive to glucose
GDP
-
31.3% decreased activity
glucokinase regulatory protein
-
wild type enzyme and mutant enzymes V62A, V62T, and V62E are significantly inhibited (80% enzyme activity remaining), no inhibition of V62L, V62M, V62Q, V62F, V62K
-
glucokinase regulatory protein
-
competitive inhibitor of glucokinase, in the fasted state, glucokinase is in part sequestered in the nucleus in an inactive state, complexed to a specific regulatory protein, glucokinase regulatory protein
-
glucokinase regulatory protein
-
-
-
glucokinase regulatory protein
-
binding of fructose 6-phosphate to glucokinase regulatory protein favors the glucokinase regulatory protein-glucokinas interaction with a negative effect on enzyme activity, while binding of fructose-1-phosphate weakens the glucokinase regulatory protein-glucokinase interaction and releases active glucokinase, the reversible association of glucokinase with glucokinase regulatory protein does more than simply regulate the catalytic activity of glucokinase, it also appears to underlie the intracellular trafficking of glucokinase between cytoplasm and nucleus
-
glucokinase regulatory protein
-
competitive inhibitor
-
glucokinase regulatory protein
-
competitive inhibitor of GCK activity, fructose 6-phoshate and fructose 1-phosphate enhance or reduce glucokinase regulatory protein-mediated inhibition, respectively. P446L-glucokinase regulatory protein has reduced regulation by physiological concentrations of fructose 6-phoshate, resulting indirectly in increased glucokinase activity
-
glucokinase regulatory protein
-
inhibits competitively GCK activity with D-glucose, inhibition of glucokinase activity by glucokinase regulatory protein in vivo is enhanced by fructose 6-phosphate or sorbitol 6-phosphate
-
glucokinase regulatory protein
-
-
-
glucokinase regulatory protein
-
binds glucokinase in the nucleus and inhibits its activity
-
glucose 1,6-disphosphate
-
-
GSSG
-
strong inhibitor at all concentrations
GSSG
-
product inhibition
I-
-
noncompetitive to glucose
I-
-
at about 0.25 M KI, 70% inhibition, reversible
Insulin
-
decreases glucokinase activity at 5.5 mM glucose and at 10 mM glucose. No effect at 2.8 mM glucose or at 20 mM glucose
-
KCl
-, Q56VN6
10 mM, 92% inhibition
KSCN
-
at about 0.25 M, 90% inhibition, reversible
Lactate
-
lactate indirectly inhibits hexokinase activity, which results from its cellular redistribution, attributed to alterations of hexokinase structure. No modulation of hexokinase activity in heart or kidney
lauric acid
Q95PL2
IC50: 0.0758 mM, TbHK1
leptin
-
decreases glucokinase activity at all glucose concentrations tested
-
lonidamine
-
lonidamine is toxic to cultured bloodstream form parasites and procyclic form parasites. Overexpression of TbHK1 protects procyclic forms from lonidamine
mannoheptulose
-
-
mannoheptulose
-
; inhibition of non-cytosolic enzyme and cytosolic enzyme
mannoheptulose
-, Q56VN6
-
Mg2+
-
at 10 mM, slight
Mg2+
-
competitive to MgATP2-; uncomplexed
Mg2+
-
competitive to MgATP2-; uncomplexed
Mg2+
-
enzyme is inhibited by an excess of free divalent metal ion, Mg2+ or Mn2+
Mg2+
-, Q56VN6
100 mM, 72% inhibition
MgADP-
-
erythrocyte enzyme, mixed inhibitor versus MgATP2- and D-glucose
MgADP-
-
product inhibition, mixed type inhibition versus MgATP2-, competitive inhibition versus 2-deoxyglucose
myristic acid
Q95PL2
IC50: 0.0784 mM, TbHK1
N-acetyl glucosamine
-, Q56VN6
-
N-acetyl-D-glucosamine
-
competitive to glucose; erythrocyte enzyme; noncompetitive to MgATP2-
N-acetyl-D-glucosamine
-
competitive to glucose
N-acetyl-D-glucosamine
-
-
N-acetyl-D-glucosamine
-
potent inhibitor of hexokinase I
N-acetylglucosamine
-
mixed versus MgATP2-, competitive inhibition versus 2-deoxyglucose
N-acetylmannosamine
-
-
N-methylglucosamine
-
potent inhibitor of hexokinase I
NaCl
-, Q56VN6
10 mM, 96% inhibition
neuropeptide Y
-
-
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
NO3-
-
noncompetitive to glucose
NO3-
-
at about 0.25 M NaNO3, 40% inhibition, reversible
oxidized glutathione
-
82.9% decreased activity
p-chloromercuribenzoate
-, Q56VN6
0.05 mM, 72% inhibition
palmitic acid
Q95PL2
IC50: 0.0624 mM, TbHK1
palmitoyl-CoA
-
inhibition of enzymes from rat liver, pig liver, Buffo marinus, no inhibition: rat brain, bovine heart, yeast
palmitoyl-CoA
-
inhibition of enzymes from rat liver, pig liver, Buffo marinus, no inhibition: rat brain, bovine heart, yeast; inhibitor binds to a site distinct from the catalytic site, noncompetitive to MgATP2-, competitive to glucose, synergistic with N-acetylglucosamine
palmitoyl-CoA
-
inhibition of enzymes from rat liver, pig liver, Buffo marinus, no inhibition: rat brain, bovine heart, yeast
palmitoyl-CoA
-
-
phosphate
-
at higher concentrations, binds to a lower affinity site in the C-terminal half, HK I and HK I+
phosphate
-
noncompetitive to glucose
phosphate
-
-
phosphate
-
competitive versus ATP; intact enzyme: at high concentrations, catalytically active 51 kDa C fragment of hexokinase: also at low concentrations; noncompetitive to glucose
phosphate
-
hexokinase III
phosphate
Q7ZAH1, -
-
phosphate
-
at high concentrations, 10-50 mM, inhibition of recombinant full-length HK I, a truncated form lacking the first 11 amino acids named HK-11aa, and of the 50 kDa C-terminal half containing the catalytic domain, competitive versus MgATP2-
phosphate
P05708
competitive versus ATP; hexokinase I, at high concentrations
phosphate
-
inhibits type II and III isozymes, synergistic with D-glucose 6-phosphate product inhibition
phosphatidylinositol
-
effectiveness of various ligands in protection against inhibition, effect of pH and temperature
phosphatidylserine
-
-
phosphoenolpyruvate
-
hexokinase III
quercetin
-
quercetin inhibition, but not binding, is relieved by glycerol 3-phosphate at pH 6.5
reduced glutathione
-
1 mM: reduced state of the enzyme with full catalytic activity, marked inhibition at high concentrations
reduced glutathione
-
54.5% decreased activity
Regulatory protein
-
inhibition of enzymes from rat liver, pig liver, Buffo marinus, no inhibition: rat brain, bovine heart, yeast
-
Regulatory protein
-
inhibition of enzymes from rat liver, pig liver, Buffo marinus, no inhibition: rat brain, bovine heart, yeast; inhibitor binds to a site distinct from the catalytic site, noncompetitive to MgATP2-, competitive to glucose, synergistic with N-acetylglucosamine, phosphate and sulfate decrease inhibition, monovalent anions antagonize inhibition with the following decreasing order of potency: I-, Br-, NO3-, Cl-, F-, acetate
-
Regulatory protein
-
inhibition of enzymes from rat liver, pig liver, Buffo marinus, no inhibition: rat brain, bovine heart, yeast
-
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
SO42-
-
noncompetitive to glucose
SO42-
-
catalytically active 51 kDa C fragment of hexokinase
Trehalose 6-phosphate
-, Q96VP5
competitive to D-glucose
Trehalose 6-phosphate
-
90.9% decreased activity
Trehalose 6-phosphate
A1Z0M7, -
-
Triethyltin bromide
-
0.5 mM, 1 h, 37C, nearly complete inhibition; selective inhibitor, sugar substrates D-glucose and D-mannose protect
Triethyltin bromide
-
selective inhibitor, sugar substrates D-glucose and D-mannose protect
UDP
-
51.9% decreased activity
UDP-glucose
-
62.5% decreased activity
Zn2+
Q5RLG0, -
slight inhibition
[[(3-bromophenyl)amino]methylene]bis(phosphonic acid)
-
mixed to non-competitive inhibitors against ATP, competitive against D-glucose
[[(9-ethyl-9H-carbazol-3-yl)amino]methylene]bis(phosphonic acid)
-
mixed to non-competitive inhibitors against ATP, competitive against D-glucose
Mn2+
-
enzyme is inhibited by an excess of free divalent metal ion, Mg2+ or Mn2+
additional information
-
not inhibited by 2-deoxy-D-glucose 6-phosphate
-
additional information
-
not inhibited by D-glucose 6-phosphate
-
additional information
-
enzymes from rat brain and bovine heart are not inhibited by palmitoyl-CoA or regulatory protein
-
additional information
-
-
-
additional information
-
not inhibited by 1 mM phosphatidylethanolamine or phosphatidylcholine
-
additional information
-
not inhibited by glyceraldehyde 3-phosphate, pyruvate, lactate
-
additional information
-
not inhibited by D-glucose 6-phosphate
-
additional information
P50521, Q09756
not inhibited by trehalose 6-phosphate; not inhibited by trehalose 6-phosphate
-
additional information
Q969A8, -
not inhibited by D-fructose 6-phosphate, ADP; not inhibited by D-glucose 6-phosphate; not inhibited by trehalose 6-phosphate
-
additional information
Q8ST54
not inhibited by D-fructose; not inhibited by D-glucose 6-phosphate; not inhibited by trehalose 6-phosphate
-
additional information
-
not inhibited by D-glucose 6-phosphate
-
additional information
-
inhibition mechanism, overview
-
additional information
-
multiplex inhibitor screening, mass spectrometry-based assay
-
additional information
P33284
inactivation by autophosphorylation at Ser157 utilizing MgATP2-, first order kinetics reaveal an extrapolated residual activity of about 60%
-
additional information
-
enzyme is not affected by D-glucose 6-phosphate; TcHK is not affected by D-glucose 6-phosphate
-
additional information
-
no inhibition by D-glucose 6-phosphate and D-trehalose 6-phosphate
-
additional information
-
D-glucose 6-phosphate has no effect on the enzyme from seed
-
additional information
-
D-glucose 6-phosphate has no effect
-
additional information
O64390, Q9SQ76
D-glucose 6-phosphate has no effect; no inhibition of hexokinase 2: D-glucose 6-phosphate
-
additional information
-
not inhibited by D-glucose 6-phosphate
-
additional information
-
no product inhibition by D-glucose 6-phosphate
-
additional information
-
not inhibited by D-glucose-6-phosphate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2E)-3-cyclopentyl-2-[4-(cyclopropylsulfonyl)phenyl]-N-[4-(1,2-dihydroxyethyl)-1,3-thiazol-2-yl]prop-2-enamide
-
-
(2R)-2-[4-(cyclopropylsulfonyl)phenyl]-N-(5-fluorothiazol-2-yl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
96% maximum activation above control at 6.5 mM glucose
(2R)-3-cyclopentyl-2-[4-(methylsulfonyl)phenyl]-N-(1,3-thiazol-2-yl)propanamide}
-
RO0281675, 1.5fold change in Vmax or kcat at 0.003 mM
(6-ethoxyquinazolin-4-yl)(1-methyl-1H-pyrazol-3-yl)amine
-
increases glucokinase activity at glucose concentrations up to approximately 20 mM
(6-ethoxyquinazolin-4-yl)pyridin-2-ylamine
-
increases glucokinase activity at glucose concentrations below approximately 7 mM
(6-isopropoxyquinazolin-4-yl)(1-methyl-1H-pyrazol-3-yl)amine
-
increases glucokinase activity at glucose concentrations up to approximately 20 mM
(R)-2-(4-(methylsulfonyl)phenyl)-3-((R)-3-oxocyclopentyl)-N-(pyrazin-2-yl)propanamide
-
piragliatin
(S)-2-(4-(cyclopropylsulfonyl)phenyl)-N-(5-fluorothiazol-2-yl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
PSN-GK1, 1.1fold change in Vmax or kcat at 0.0001 mM
(S)-2-[3-chloro-4-(ethylsulfonyl)-2-oxopyridin-1(2H)-yl]-N-(5-methylpyridin-2-yl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
26% maximum activation above control at 6.5 mM glucose
(S)-2-[3-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-(4,4-difluorocyclohexyl)-N-(5-methylpyridin-2-yl)propanamide
-
15% maximum activation above control at 6.5 mM glucose
(S)-2-[3-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclobutyl-N-(5-methylpyridin-2-yl)propanamide
-
72% maximum activation above control at 6.5 mM glucose
(S)-2-[3-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclohexyl-N-(5-methylpyridin-2-yl)propanamide
-
46% maximum activation above control at 6.5 mM glucose
(S)-2-[3-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(5-methylpyridin-2-yl)propanamide
-
57% maximum activation above control at 6.5 mM glucose
(S)-2-[3-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-4-methyl-N-(5-methylpyridin-2-yl)pentanamide
-
37% maximum activation above control at 6.5 mM glucose
(S)-2-[3-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-N-(5-methylpyridin-2-yl)-3-phenylpropanamide
-
30% maximum activation above control at 6.5 mM glucose
(S)-2-[4-(cyclobutylsulfonyl)-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(5-methylpyridin-2-yl)propanamide
-
67% maximum activation above control at 6.5 mM glucose
(S)-2-[4-(cyclobutylsulfonyl)-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-pyrazin-2-ylpropanamide
-
66% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-(cyclobutylsulfonyl)-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(1-methyl-1H-pyrazol-3-yl)propanamide
-
67% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-(cyclopropylsulfonyl)-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(1-methyl-1H-pyrazol-3-yl)propanamide
-
84% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-(methylsulfonyl)-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(5-methylpyridin-2-yl)propanamide
-
122% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-(methylsulfonyl)-2-oxopyridin-1(2H)-yl]-N-(5-chloropyridin-2-yl)-3-cyclopentylpropanamide
-
82% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(1-methyl-1H-pyrazol-3-yl)propanamide
-
57% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(5-methylpyrazin-2-yl)propanamide
-
104% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(5-methylpyridin-2-yl)propanamide
-
69% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-1,3-thiazol-2-ylpropanamide
-
42% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-1H-pyrazol-3-ylpropanamide
-
50% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-2-[4-(cyclopropylsulfonyl)-2-oxopyridin-1(2H)-yl]-N-(5-methylpyridin-2-yl)propanamide
-
76% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-2-[4-(cyclopropylsulfonyl)-2-oxopyridin-1(2H)-yl]-N-pyrazin-2-ylpropanamide
-
94% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-2-[4-(ethylsulfonyl)-2-oxopyridin-1(2H)-yl]-N-(5-methylpyridin-2-yl)propanamide
-
73% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-2-[4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-N-(5-methylpyridin-2-yl)propanamide
-
65% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-2-[4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-N-pyridin-2-ylpropanamide
-
43% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-2-[4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-N-[5-(trifluoromethyl)pyridin-2-yl]propanamide
-
35% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-2-[5-methyl-4-(methylsulfonyl)-2-oxopyridin-1(2H)-yl]-N-(5-methylpyridin-2-yl)propanamide
-
103% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-2-[5-methyl-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-N-(5-methylpyridin-2-yl)propanamide
-
48% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-N-(5-methylpyrazin-2-yl)-2-[4-(methylsulfonyl)-2-oxopyridin-1(2H)-yl]propanamide
-
101% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-N-(5-methylpyridin-2-yl)-2-[4-(methylsulfonyl)-2-oxopyridin-1(2H)-yl]propanamide
-
58% maximum activation above control at 6.5 mM glucose
1-(1-(4-chlorophenyl)cyclohexyl)-3-(thiazol-2-yl)urea
-
-
2-(methylamino)-N-(4-methyl-1,3-thiazol-2-yl)-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
-
-
2-amino-4-chloro-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-4-fluoro-5-((1-methyl-1H-imidazol-2-yl)thio)-N-(thiazol-2-yl)benzamide
-
-
2-amino-4-fluoro-5-((1-methyl-1H-imidazol-2-yl)thio)-N-(thiazol-2-yl)benzamide
-
1.6fold change in Vmax or kcat at 0.03 mM
2-amino-4-fluoro-5-(1,3,4-thiadiazol-2-ylsulfanyl)-N-(3-trifluoromethyl-phenyl)-benzamide
-
1.14fold activation at 0.01 mM
2-amino-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-N-(3-trifluoromethyl-phenyl)-benzamide
-
1.47fold activation at 0.01 mM
2-amino-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-N-thiazol-2-yl-benzamide
-
-
2-amino-4-fluoro-5-(4-methyl-thiazol-2-ylsulfanyl)-N-(3-trifluoromethyl-phenyl)-benzamide
-
0.89fold activation at 0.01 mM
2-amino-4-fluoro-5-(thiazol-2-ylsulfanyl)-N-(3-trifluoromethyl-phenyl)-benzamide
-
1.15fold activation at 0.01 mM
2-amino-4-fluoro-5-[(1-methyl-1H-imidazol-2-yl)sulfanyl]-N-(4-methylthiazol-2-yl)benzamide
-
108% maximum activation above control at 6.5 mM glucose
2-amino-4-fluoro-N-(3-fluoro-phenyl)-5-(1,3,4-thiadiazol-2-ylsulfanyl)-benzamide
-
1.36fold activation at 0.01 mM
2-amino-4-fluoro-N-(3-fluoro-phenyl)-5-(1-methyl-1Himidazol-2-ylsulfanyl)-benzamide
-
2.04fold activation at 0.01 mM
2-amino-4-fluoro-N-(3-fluoro-phenyl)-5-(pyridin-2-ylsulfanyl)-benzamide
-
1.1fold activation at 0.01 mM
2-amino-4-fluoro-N-(3-fluoro-phenyl)-5-(thiazol-2-ylsulfanyl)-benzamide
-
1.25fold activation at 0.01 mM
2-amino-4-fluoro-N-(3-methoxy-phenyl)-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
-
1.15fold activation at 0.01 mM
2-amino-4-fluoro-N-(4-methoxy-phenyl)-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
-
2.01fold activation at 0.01 mM
2-amino-5-((4-methyl-4H-1,2,4-triazol-3-yl)thio)-N-(5-methylthiazol-2-yl)benzamide
-
1.3fold change in Vmax or kcat at 0.01 mM
2-amino-5-(1H-imidazol-2-ylsulfanyl)-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-(2-fluorophenoxy)-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-(2-methoxyphenoxy)-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-(3-fluorophenoxy)-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-(4-fluorophenoxy)-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-(benzoxazol-2-ylsulfanyl)-4-fluoro-N-(3-fluoro-phenyl)-benzamide
-
0.83fold activation at 0.01 mM
2-amino-5-(ethylsulfanyl)-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-chloro-N-(1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-chloro-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-ethoxy-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-[(1-methyl-1H-imidazol-2-yl)sulfanyl]-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]-N-(1,2,4-thiadiazol-5-yl)benzamide
-
-
2-amino-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]-N-(1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]-N-[4-(trifluoromethyl)-1,3-thiazol-2-yl]benzamide
-
-
2-amino-5-[2-[methyl(methylidene)oxido-l6-sulfanyl]phenoxy]-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-N-(1,3-thiazol-2-yl)benzamide
-
-
2-amino-N-(3,4-dimethoxy-phenyl)-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
-
1.32fold activation at 0.01 mM
2-amino-N-(3-amino-phenyl)-4-fluoro-5-(1,3,4-thiadiazol-2-ylsulfanyl)-benzamide
-
1.22fold activation at 0.01 mM
2-amino-N-(3-amino-phenyl)-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
-
2.09fold activation at 0.01 mM
2-amino-N-(3-amino-phenyl)-4-fluoro-5-(4-methylthiazol-2-ylsulfanyl)-benzamide
-
1.1fold activation at 0.01 mM
2-amino-N-(3-amino-phenyl)-4-fluoro-5-(pyridin-2-ylsulfanyl)-benzamide
-
1.12fold activation at 0.01 mM
2-amino-N-(3-amino-phenyl)-4-fluoro-5-(thiazol-2-ylsulfanyl)-benzamide
-
1.21fold activation at 0.01 mM
2-amino-N-(3-amino-phenyl)-5-(4,6-dimethyl-pyrimidin-2-ylsulfanyl)-4-fluoro-benzamide
-
1.09fold activation at 0.01 mM
2-amino-N-(3-aminomethyl-phenyl)-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
-
1.01fold activation at 0.01 mM
2-amino-N-(3-cyano-phenyl)-4-fluoro-5-(1,3,4-thiadiazol-2-ylsulfanyl)-benzamide
-
1.2fold activation at 0.01 mM
2-amino-N-(3-cyano-phenyl)-4-fluoro-5-(1-methyl-1Himidazol-2-ylsulfanyl)-benzamide
-
1.95fold activation at 0.01 mM
2-amino-N-(3-cyano-phenyl)-4-fluoro-5-(4-methylthiazol-2-ylsulfanyl)-benzamide
-
0.99fold activation at 0.01 mM
2-amino-N-(3-cyano-phenyl)-4-fluoro-5-(thiazol-2-ylsulfanyl)-benzamide
-
1.2fold activation at 0.01 mM
2-amino-N-(3-cyano-phenyl)-5-(4,6-dimethyl-pyrimidin-2-ylsulfanyl)-4-fluoro-benzamide
-
1.01fold activation at 0.01 mM
2-amino-N-(3-methyl-1,2,4-thiadiazol-5-yl)-5-(phenylsulfanyl)benzamide
-
-
2-amino-N-(3-methyl-1,2,4-thiadiazol-5-yl)-5-(pyridin-2-ylsulfanyl)benzamide
-
-
2-amino-N-(3-methyl-1,2,4-thiadiazol-5-yl)-5-(pyridin-3-ylsulfanyl)benzamide
-
-
2-amino-N-(3-methyl-1,2,4-thiadiazol-5-yl)-5-(pyridin-4-ylsulfanyl)benzamide
-
-
2-amino-N-(3-methyl-1,2,4-thiadiazol-5-yl)-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
-
-
2-amino-N-(4-methyl-1,3-thiazol-2-yl)-5-(4H-1,2,4-triazol-3-ylsulfanyl)benzamide
-
-
2-amino-N-(4-methyl-1,3-thiazol-2-yl)-5-(phenylsulfanyl)benzamide
-
-
2-amino-N-(4-methyl-1,3-thiazol-2-yl)-5-(pyridin-2-ylsulfanyl)benzamide
-
-
2-amino-N-(4-methyl-1,3-thiazol-2-yl)-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
-
-
2-amino-N-(4-methyl-1,3-thiazol-2-yl)-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
-
-
2-amino-N-(4-methylthiazol-2-yl)-5-phenoxybenzamide
-
-
2-amino-N-(5-methyl-1,3-thiazol-2-yl)-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
-
-
2-amino-N-[4-(hydroxymethyl)-1,3-thiazol-2-yl]-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
-
-
2-cyclopentyl-1-(4-(methylsulfonyl)phenyl)-N-(thiazol-2-yl)ethanesulfonamide
-
-
2-[(3-cyclopentyl-2-[4-[(4-methylpiperazin-1-yl)sulfonyl]phenyl]propanoyl)amino]-5-methoxy-1H-[1,3]thiazolo[5,4-b]pyridin-3-ium
-
-
2-[4-(2,4-difluoro-phenyl)-piperazin-1-yl]-N-(3,4-dimethoxy-phenyl)-acetamide
-
1.01fold activation at 0.01 mM
2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-N-(3-trifluoromethyl-phenyl)-acetamide
-
1.06fold activation at 0.01 mM
3-(5-chloro-1,3-thiazol-2-yl)-1-[4-(methylsulfonyl)phenyl]-1-(thiophen-2-ylmethyl)urea
-
-
3-(5-chlorothiazol-2-yl)-1-(4-(methylsulfonyl)phenyl)-1-(thiophen-3-ylmethyl)urea
-
-
3-amino-N-[2-amino-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-phenyl]-benzamide
-
1.16fold activation at 0.01 mM
3-phosphoglycerate
-
activates
4-[4-(dimethylcarbamoyl)-3-fluorophenoxy]-2-ethyl-2-methyl-N-(5-methylpyridin-2-yl)-2,3-dihydro-1-benzofuran-6-carboxamide
-
-
5-(2-methylpropyl)-N-(1,3-thiazol-2-yl)-1H-indazol-3-amine
-
-
5-({3-(propan-2-yloxy)-5-[2-(thiophen-3-yl)ethoxy]benzoyl}amino)-1,3,4-thiadiazole-2-carboxylic acid
-
-
6-(3-(((S)-1-methoxypropan-2-yl)oxy)-5-(((S)-1-phenylpropan-2-yl)oxy)benzamido)nicotinic acid
-
23% maximum activation above control at 6.5 mM glucose
6-(3-(((S)-1-methoxypropan-2-yl)oxy)-5-(((S)-1-phenylpropan-2-yl)oxy)benzamido)nicotinic acid
-
GKA50, 0.94fold change in Vmax or kcat at 0.03 mM
6-({3-(propan-2-yloxy)-5-[2-(thiophen-3-yl)ethoxy]benzoyl}amino)pyridine-3-carboxylic acid
-
GKA22
6-ethoxy-N-(1-methyl-1H-pyrrol-3-yl)-quinazolin-4-amine
-
0.95fold change in Vmax or kcat at 0.05 mM
6-ethoxy-N-(pyridin-2-yl)-quinazolin-4-amine
-
0.62fold change in Vmax or kcat at 0.05 mM
6-isopropoxy-N-(1-methyl-1H-pyrrol-3-yl)quinazolin-4-amine
-
0.8fold change in Vmax or kcat at 0.05 mM
6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
-
6-{[3-(2-methylpropoxy)-5-(propan-2-yloxy)benzoyl]amino}pyridine-3-carboxylic acid
-
-
alpha-D-glucose
-
-
bad peptide
-
-
-
citrate
-
allosteric activator
ethyl 2-[([2-amino-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]phenyl]carbonyl)amino]-1,3-thiazole-4-carboxylate
-
-
galactose
-
activates isoenzyme Hex II
glucokinase-associated phosphatase
-
-
-
glucokinase-associated protein
-
stimulates glucokinase activity by 30-40% when present at a 3-5fold molar excess and 2.5fold at a 50fold molar excess
-
glucose 6-phosphate
-
recombinant HXK1: at 10 mM 13% activation, at 20 mM 31% activation, recombinant HXK2: at 10 mM 23% activation, at 20 mM 48% activation
glucose-6-phosphate
-, Q56VN6
10 mM, recombinant enzyme is 3fold activated
glycerol 3-phosphate
-
influences enzyme activity at pH 6.5 by preventing substrate and product inhibition by ATP and ADP, respectively
Insulin
-
stimulating effect is abolished when lactate is added
-
Isocitrate
-
activates isoenzyme Hex II
LY-2121260
-
addition of 0.02 mM LY-2121260 results in the loss of positive cooperativity with glucose and in activation of glucokinase catalysis increasing both kcat and the apparent glucose affinity
lyxose
-
activates isoenzyme Hex II
N,N'-bis-(2-methoxy-phenyl)-isophthalamide
-
1.02fold activation at 0.01 mM
N,N'-bis-(3-methoxy-phenyl)-isophthalamide
-
0.81fold activation at 0.01 mM
N,N'-bis-(4-methoxy-phenyl)-isophthalamide
-
0.89fold activation at 0.01 mM
N,N-dicyclohexyl-N'-methyldicarbonimidic diamide
-
-
N-(3-amino-phenyl)-2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-acetamide
-
1.08fold activation at 0.01 mM
N-(3-cyano-phenyl)-2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-acetamide
-
0.96fold activation at 0.01 mM
N-(3-fluoro-phenyl)-2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-acetamide
-
1.01fold activation at 0.01 mM
N-(4-methyl-1,3-thiazol-2-yl)-3-(pyridin-3-ylmethoxy)pyridin-2-amine
-
-
N-(4-methyl-1,3-thiazol-2-yl)-3-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
-
-
N-(4-methyl-1,3-thiazol-2-yl)-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]-2-nitrobenzamide
-
-
N-[2-amino-4-fluoro-5-[(1-methyl-1H-imidazol-2-yl)sulfanyl]benzyl]-1,3-thiazol-2-amine
-
addition of 0.02 mM N-[2-amino-4-fluoro-5-[(1-methyl-1H-imidazol-2-yl)sulfanyl]benzyl]-1,3-thiazol-2-amine results in the loss of positive cooperativity with glucose and in activation of glucokinase catalysis increasing both kcat and the apparent glucose affinity
pentaubiquitin
-
the recombinant glucokinase is allosterically activated up to 1.4fold by purified free pentaubiquitin chains at about 100 nM, and possibly also by unidentified polyubiquitinated proteins
-
pentaubiquitin
-
-
-
phosphate
-
activates
phosphoenolpyruvate
-
activates isoenzyme Hex I
polyubiquitin
-
causes modest activation
-
propionyl-CoA carboxylase beta-subunit
-
-
-
ribose
-
activates isoenzyme Hex II
RO-0275145
-
-
RO-0281675
-
81% maximum activation above control at 6.5 mM glucose
RO-1440
-
148% maximum activation above control at 6.5 mM glucose
RO-281675
-
-
RO-4389620
-
also known as R1440, GK2, or piragliatin
RO0274375
-
wild-type enzyme V62A, V62T, and V62L respond to the activator. V62Q, V62E, V62F, and V62K are resistant to the activators
RO0283946
-
wild-type enzyme V62A, V62T, and V62L respond to the activator. V62Q, V62E, V62F, and V62K are resistant to the activators
-
RO281675
-
wild-type enzyme V62A, V62T, and V62L respond to the activator. V62Q, V62E, V62F, and V62K are resistant to the activators
xylose
-
activates isoenzyme Hex II
mannose 6-phosphate
-
activates isoenzyme Hex II
additional information
P50521, Q09756
hxk1+ expression increases strongly during growth in fructose or glycerol; hxk2+ expression is highest during growth in glycerol
-
additional information
-
increased activity of the cytosolic and non-cytosolic isozymes induced by tobacco mosaic virus TMV
-
additional information
-
the allosteric activator compound A, increases the level of cytoplasmic glucokinase in both isolated rat primary hepatocytes and the liver tissues from rats. Compound A interacts with glucose-bound free GK, thereby impairing the association of glucokinase and glucokinase regulatory protein
-
additional information
-
not affected by 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
20
-
1,5-Anhydro-D-glucitol
-
at 37C, pH 7.4
5
-
1-thio-D-glucose
-
at 37C, pH 7.4
-
0.2
-
2-deoxy-2-fluoroglucose
-
at 37C, pH 7.4
0.033
-
2-deoxy-D-glucose
-
hexokinase III, at 30C, pH 8.1
0.1
-
2-deoxy-D-glucose
-
rat brain enzyme, hexokinase I
0.125
-
2-deoxy-D-glucose
-
-
0.125
-
2-deoxy-D-glucose
-
bovine heart enzyme, hexokinase II
0.134
-
2-deoxy-D-glucose
-
at 30C, pH 8.1
0.152
-
2-deoxy-D-glucose
-
HKI, at 25C, pH 7.4
0.18
-
2-deoxy-D-glucose
-
HKI, at 25C, pH 7.4
0.187
-
2-deoxy-D-glucose
Q7ZAH1, -
at 50C, pH 7.5
0.33
-
2-deoxy-D-glucose
-
90C, pH 6.2
0.44
-
2-deoxy-D-glucose
-
pH 7.5, 50C, ATP as phosphoryl donor
0.5
-
2-deoxy-D-glucose
-
hexokinase I, at 37C, pH 8.1
0.56
-
2-deoxy-D-glucose
-
hexokinase Ib, at 37C, pH 7.2
0.613
-
2-deoxy-D-glucose
-
HKII, at 25C, pH 7.4
0.77
-
2-deoxy-D-glucose
-
hexokinase Ia, at 37C, pH 7.2
0.9
-
2-deoxy-D-glucose
-
hexokinase Ia
1.16
-
2-deoxy-D-glucose
-
hexokinase Ic, at 37C, pH 7.2
1.33
-
2-deoxy-D-glucose
-
erythrocyte enzyme
2
-
2-deoxy-D-glucose
-
hexokinase Ib
2
-
2-deoxy-D-glucose
-
at 37C, pH 8.1
3.6
-
2-deoxy-D-glucose
-
-
9
-
2-deoxy-D-glucose
-
rat liver enzyme, hexokinase IV
19.2
-
2-deoxy-D-glucose
-
pH 8.0, 30C
0.055
0.062
2-fluoro-2-deoxy-D-glucose
-
HK I, at 25C, pH 7.4
0.068
0.077
2-fluoro-2-deoxy-D-glucose
-
HK I, at 25C, pH 7.4
0.166
0.174
2-fluoro-2-deoxy-D-glucose
-
HK II, at 25C, pH 7.4
30
-
3-deoxy-3-amino-D-glucose
-
at 37C, pH 7.4
4
-
5-thio-D-glucose
-
-
0.03054
-
ATP
B8K2W7, -
pH 7.6, 22C
0.061
-
ATP
Q3S2I3, -
30C, pH 8.0
0.06948
-
ATP
B8K2W7, -
pH 8.2, 22C
0.07
-
ATP
-
mutant enzyme V62E
0.075
-
ATP
-
MgATP2-, bound mitochondrial HK I, at pH 7.5
0.08816
-
ATP
B8K2W7, -
pH 7.0, 22C
0.09
-
ATP
-
HK1
0.1
-
ATP
-
pH 7.5, 22C
0.11
-
ATP
-
mutant enzyme V62Q
0.12
-
ATP
-
pH 7.5, 50C, D-glucose as phosphoryl acceptor
0.125
-
ATP
-
MgATP2-, at 30C, pH 8.1
0.14
-
ATP
-
cosubstrate: glucose, wild-type enzyme
0.16
-
ATP
-
mutant enzyme V62K
0.181
-
ATP
-
MgATP2-, solubilized mitochondrial HK I, at pH 7.5
0.183
-
ATP
-
recombinant HXK1, at 30C, pH 8
0.2
-
ATP
-
-
0.2
-
ATP
-
mutant enzyme V62A
0.208
-
ATP
-
MgATP2-
0.22
-
ATP
-
mutant enzyme V62T
0.22
-
ATP
-
pH 6.5, temperature not specified in the publication
0.226
-
ATP
P33284
pH 7.4, 25C, recombinant enzyme at 0.001 mg/ml
0.239
-
ATP
-
control, pH 8.2, 25C, 250 mM glucose
0.248
-
ATP
-
control, pH 8.2, 25C; control, pH 8.2, 25C, no glucose
0.257
-
ATP
-
control, pH 8.2, 5C, 250 mM glucose
0.28
-
ATP
-
HK2
0.28
-
ATP
-
pH 7.5
0.28
-
ATP
Q95PL2
recombinant TbHK1
0.28
-
ATP
-
30C, mutant enzyme A456V
0.28
-
ATP
-
pH 7.4, temperature not specified in the publication
0.29
-
ATP
Q7ZAH1, -
at 50C, pH 7.5
0.29
-
ATP
-
37C, pH 7.4, mutant enzyme A456V
0.29
-
ATP
-
30C, mutant enzyme >214C
0.3
-
ATP
-
recombinant hexokinase I expressed in Escherichia coli
0.3
-
ATP
-
hexokinase II, at 30C, pH 8.1
0.3
-
ATP
P19367
wild type enzyme, in 25 mM HEPES (pH 7.1), at 25C
0.32
0.38
ATP
Q8ST54
natural and recombinant hexokinase, expressed in Escherichia coli XL-1 Blue, at pH 7.5
0.33
-
ATP
-
frozen, pH 8.2, 25C; frozen, pH 8.2, 25C, no glucose
0.336
-
ATP
-
frozen, pH 8.2, 5C, 250 mM glucose
0.342
-
ATP
-
frozen, pH 8.2, 25C, 250 mM glucose
0.364
-
ATP
-
control, pH 8.2, 5C, no glucose
0.39
-
ATP
P33284
pH 7.4, 25C, recombinant enzyme at 1.0 mg/ml
0.39
-
ATP
-
37C, pH 7.4, wild-type enzyme
0.4
-
ATP
-
hexokinase B
0.41
-
ATP
-
wild-type enzyme
0.41
-
ATP
-
30C, wild-type enzyme
0.42
-
ATP
-
90C, pH 6.2
0.43
0.47
ATP
P05708
recombinant wild-type hexokinase I, D84A, D84E and D84K mutants
0.43
-
ATP
-
30C, mutant enzyme A208G
0.44
-
ATP
-
hexokinase II
0.45
0.47
ATP
-
HK I and its D84A mutant
0.46
-
ATP
-
mutant enzyme V62M
0.5
-
ATP
-
MgATP2-; reticulocyte and erythrocyte enzymes
0.5
-
ATP
-
at 30C, pH 7.5
0.5
-
ATP
-
MgATP2-; reticulocyte hexokinase Ia and Ib, at 37C, pH 8.1
0.5
-
ATP
-
hexokinase III, at 30C, pH 8.1
0.5
-
ATP
-
type I isozyme
0.505
-
ATP
-
frozen, pH 8.2, 5C, no glucose
0.51
-
ATP
-
MgATP2-
0.55
-
ATP
-
30C, mutant enzyme A460R
0.56
-
ATP
-
HK3
0.58
0.62
ATP
-
MgATP2-, hexokinases Ia, Ib and Ic, at 37C, pH 7.2
0.6
-
ATP
-
MgATP2-, erythrocyte enzyme
0.6
-
ATP
-
hexokinase C
0.6
-
ATP
-
MgATP, hexokinase I, at 37C, pH 8.1
0.6
-
ATP
-
30C, mutant enzyme K459L
0.61
-
ATP
-
mutant enzyme V62L
0.62
-
ATP
-
MgATP2-, at 37C, pH 8.1
0.65
-
ATP
-
30C, mutant enzyme C457V; 30C, mutant enzyme Y215A
0.654
-
ATP
-
recombinant HXK2, at 30C, pH 8
0.66
1.2
ATP
P19367
wild-type and nonaggregating interface mutant hexokinase I, pH 7.8
0.7
-
ATP
-
type II isozyme
0.7
-
ATP
-
wild type enzyme, at 30C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
0.7
-
ATP
-
wild type enzyme, at 25C
0.71
-
ATP
-
hexokinase III
0.71
-
ATP
-
mutant enzyme V62F
0.77
-
ATP
-
wild type enzyme, at 37C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
0.81
-
ATP
-
30C, mutant enzyme K458R
0.81
-
ATP
-
wild type hexokinase II
0.82
-
ATP
-
mutant enzyme V62M, at 30C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
0.85
-
ATP
-
mutant enzyme V62M, at 37C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
0.93
-
ATP
-
at pH 8.5
1
-
ATP
-
type III isozyme
1.05
-
ATP
Q969A8, -
at 37C, pH 7
1.09
-
ATP
-
pH 8.0, wild-type enzyme
1.09
-
ATP
-, Q56VN6
-
1.1
1.4
ATP
-
MgATP2-, recombinant HK I, a truncate HK I form lacking the first 11 amino acids named HK-11aa, and the 50 kDa C-terminal half of HK I, at 37C, pH 7.2
1.1
-
ATP
-
mutant enzyme G72R, at 30C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol; mutant enzyme G72R, at 37C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
1.16
-
ATP
-
pH 8.0, mutant enzyme A464P/E465G
1.25
-
ATP
-
hexokinase III from lymphocytes, at 37C, pH 8.1
1.3
1.4
ATP
-
HK I+ and its D84A mutant
1.51
-
ATP
-
pH 8.0, mutant enzyme Q466_H467insHMNLAEQ
1.73
-
ATP
-
37C, pH 7.4, mutant enzyme K414E
3.05
-
ATP
-
catalytically active recombinant carboxyl-domain of hexokinase III, at 37C, pH 8.1
0.52
-
CTP
-
pH 7.5, 50C, D-glucose as phosphoryl acceptor
1.993
-
CTP
B8K2W7, -
pH 7.6, 22C
2
-
CTP
Q3S2I3, -
30C, pH 8.0
2.317
-
CTP
B8K2W7, -
pH 8.2, 22C
5
-
CTP
-
MgCTP2-, hexokinase I, at 37C, pH 8.1
0.025
-
D-fructose
-, Q6Q8A5
pH 8.4, 30C, recombinant isozyme hexokinase 2
0.035
-
D-fructose
Q95PL2
recombinant TbHK1
0.142
-
D-fructose
-
-
0.15
-
D-fructose
-
90C, pH 6.2
0.23
-
D-fructose
-
-
0.33
-
D-fructose
-
hexokinases PI and PII
0.47
-
D-fructose
-
isozyme HKII
0.5
-
D-fructose
-
41C, pH 7.5
0.7
-
D-fructose
A1Z0M7, -
-
0.734
-
D-fructose
Q7ZAH1, -
at 50C, pH 7.5
0.9
-
D-fructose
-
at 30C, pH 7.5
1
-
D-fructose
-
-
1.1
-
D-fructose
-, Q96VP5
pH 7.5, 37C
1.44
-
D-fructose
-
at 30C, pH 8.1
1.5
-
D-fructose
-
hexokinase III, at 30C, pH 8.1
1.5
-
D-fructose
P50521, Q09756
;
2
-
D-fructose
-
25C, pH 7.5
2.5
-
D-fructose
-
isozyme HKI
2.9
-
D-fructose
-
; S-nitrosoglutathione treated enzyme
3.625
-
D-fructose
B8K2W7, -
pH 7.0, 22C
4
-
D-fructose
-
hexokinase Ia
4.5
-
D-fructose
-
at 37C, pH 8.1
4.567
-
D-fructose
B8K2W7, -
pH 7.6, 22C
5.145
-
D-fructose
B8K2W7, -
pH 8.2, 22C
5.2
-
D-fructose
Q3S2I3, -
30C, pH 8.0
8.7
-
D-fructose
-
HK3
9.3
-
D-fructose
-
hexokinase
10
13
D-fructose
-
hexokinases Ia, Ib and Ic, at 37C, pH 7.2
11
-
D-fructose
-
HK1
11.4
-
D-fructose
-
hexokinase I, at 37C, pH 8.1
17.8
-
D-fructose
-
erythrocyte enzyme
22
-
D-fructose
-
HK2
25
-
D-fructose
-
hexokinase Ib
29
-
D-fructose
-
-
30
-
D-fructose
-
pH 7.5, 50C, ATP as phosphoryl donor
75
-
D-fructose
-, Q56VN6
-
80
-
D-fructose
-
-
157.7
-
D-fructose
-
30C, pH 7.5
1510
-
D-fructose
Q5SLJ4, -
pH 7.0, 50C
105
-
D-galactose
Q5SLJ4, -
pH 7.0, 50C
0.06
-
D-glucosamine
-
at 30C, pH 7.5
0.06
-
D-glucosamine
-
90C, pH 6.2
0.116
-
D-glucosamine
-
at 30C, pH 8.1
0.2
-
D-glucosamine
-
hexokinase III, at 30C, pH 8.1
0.23
-
D-glucosamine
-
pH 7.5, 50C, ATP as phosphoryl donor
0.4
-
D-glucosamine
-
at 37C, pH 8.1
0.5
-
D-glucosamine
-
hexokinases Ib and Ic, at 37C, pH 7.2
0.6
-
D-glucosamine
-
hexokinase I, at 37C, pH 8.1
0.85
-
D-glucosamine
-
hexokinase Ia
1.3
-
D-glucosamine
-
hexokinase Ib
1.5
-
D-glucosamine
-
hexokinase Ia, at 37C, pH 7.2
2
-
D-glucosamine
-
erythrocyte enzyme
0.003
-
D-glucose
-
type III isozyme
0.008
-
D-glucose
Q969A8, -
at 37C, pH 7
0.009
-
D-glucose
Q95PL2
recombinant TbHK1
0.012
-
D-glucose
-
at 30C, pH 8.1
0.015
-
D-glucose
-
hexokinase III, at 30C, pH 8.1
0.023
-
D-glucose
-
-
0.023
-
D-glucose
Q3S2I3, -
30C, pH 8.0
0.025
-
D-glucose
-
hexokinase C
0.03
-
D-glucose
-
type I isozyme
0.032
0.034
D-glucose
-
HK I, at 25C, pH 7.4
0.032
-
D-glucose
-
recombinant hexokinase I expressed in Escherichia coli
0.0338
-
D-glucose
B8K2W7, -
pH 7.0, 22C
0.034
-
D-glucose
-
hexokinase III from lymphocytes, at 37C, pH 8.1
0.034
-
D-glucose
B8K2W7, -
pH 8.2, 22C
0.035
0.038
D-glucose
P05708
recombinant wild-type hexokinase I, D84A, D84E and D84K mutants
0.035
-
D-glucose
-
HK3
0.035
-
D-glucose
-
hexokinase III
0.035
-
D-glucose
-, Q56VN6
-
0.038
-
D-glucose
-
catalytically active recombinant carboxyl-domain of hexokinase III, at 37C, pH 8.1
0.03872
-
D-glucose
B8K2W7, -
pH 7.6, 22C
0.039
-
D-glucose
-
HK I, at 25C, pH 7.4
0.04
-
D-glucose
-
reticulocyte hexokinase Ia
0.04
-
D-glucose
-
glucokinase
0.04
-
D-glucose
-
at 37C, pH 8.1; reticulocyte hexokinase Ia
0.041
-
D-glucose
-
HK1
0.043
-
D-glucose
Q8ST54
natural hexokinase from epimastigotes, at pH 7.5
0.044
-
D-glucose
-
90C, pH 6.2
0.046
0.048
D-glucose
-
hexokinases Ia, Ib and Ic, at 37C, pH 7.2
0.047
-
D-glucose
-
recombinant HXK2, at 30C, pH 8
0.047
-
D-glucose
Q5W5U3
pH 7.2, 37C, recombinant catalytic C-terminal domain
0.05
0.053
D-glucose
-
HK I, HKI+ and their D84A mutants
0.05
-
D-glucose
-
at 30C, pH 7.5
0.05
-
D-glucose
-
pH 7.5
0.05
-
D-glucose
-
pH 7.5, 50C, ATP as phosphoryl donor
0.057
0.061
D-glucose
P19367
wild-type and nonaggregating interface mutant hexokinase I, pH 7.8
0.058
-
D-glucose
Q7ZAH1, -
at 50C, pH 7.5
0.059
-
D-glucose
-
recombinant HXK1, at 30C, pH 8
0.06
0.065
D-glucose
-
recombinant HK I, a truncate HK I form lacking the first 11 amino acids named HK-11aa, and the 50 kDa C-terminal half of HK I, at 37C, pH 7.2
0.06
-
D-glucose
-
erythrocyte enzyme
0.06
-
D-glucose
-
-
0.06
-
D-glucose
-
-
0.06
-
D-glucose
-
hexokinase I, at 37C, pH 8.1
0.06
-
D-glucose
Q8ST54
recombinant hexokinase expressed in Escherichia coli XL-1 Blue, at pH 7.5
0.06
-
D-glucose
-, Q6Q8A5
pH 8.4, 30C, recombinant isozyme hexokinase 2
0.062
0.065
D-glucose
-
bound and solubilized mitochondrial HK I, at pH 7.5
0.065
-
D-glucose
-
pH 8.0, mutant enzyme A464P/E465G
0.066
-
D-glucose
-
-
0.072
-
D-glucose
Q5W5U3
pH 7.2, 37C, recombinant full length enzyme
0.0732
-
D-glucose
-
pH 8.0, wild-type enzyme
0.08
-
D-glucose
-
at 37C, pH 8.1
0.0841
-
D-glucose
-
pH 8.0, mutant enzyme Q466_H467insHMNLAEQ
0.09
-
D-glucose
-
-
0.12
-
D-glucose
-
hexokinases PI and PII
0.125
-
D-glucose
-
reticulocyte hexokinase Ib
0.125
-
D-glucose
-
at 37C, pH 8.1; reticulocyte hexokinase Ib
0.129
0.137
D-glucose
-
HK II, at 25C, pH 7.4
0.13
-
D-glucose
-
-
0.13
-
D-glucose
-
HK2
0.13
-
D-glucose
-
at pH 8.5
0.13
-
D-glucose
-
pH 7.5, 22C
0.132
-
D-glucose
A1Z0M7, -
-
0.139
-
D-glucose
-
control, pH 8.2, 5C, no glucose
0.14
-
D-glucose
-
-
0.144
-
D-glucose
-
control, pH 8.2, 25C; control, pH 8.2, 25C, no glucose
0.146
-
D-glucose
-
hexokinase II
0.15
-
D-glucose
-
hexokinase II, at 30C, pH 8.1
0.16
-
D-glucose
-
hexokinase B
0.16
-
D-glucose
P50521, Q09756
-
0.196
-
D-glucose
P33284
pH 7.4, 25C, recombinant enzyme at 0.001 mg/ml
0.23
-
D-glucose
-
mutant enzyme Y214C
0.248
-
D-glucose
-
frozen, pH 8.2, 25C; frozen, pH 8.2, 25C, no glucose
0.253
-
D-glucose
-
frozen, pH 8.2, 5C, no glucose
0.26
-
D-glucose
-, Q96VP5
pH 7.5, 37C
0.28
-
D-glucose
Q5SLJ4, -
pH 7.0, 50C
0.3
-
D-glucose
-
type II isozyme
0.3
-
D-glucose
-
S-nitrosoglutathione treated enzyme
0.31
-
D-glucose
A0SZU9
-
0.37
-
D-glucose
-
wild type hexokinase II
0.451
-
D-glucose
P33284
pH 7.4, 25C, recombinant enzyme at 1.0 mg/ml
0.463
-
D-glucose
-
-
0.63
-
D-glucose
-
wild type enzyme, at 25C, in the presence of 0.02 mM activator LY-2121260
0.76
-
D-glucose
-
wild type enzyme, at 25C, in the presence of 0.02 mM activator N-[2-amino-4-fluoro-5-[(1-methyl-1H-imidazol-2-yl)sulfanyl]benzyl]-1,3-thiazol-2-amine
0.98
-
D-glucose
-
hexokinase
1.25
-
D-glucose
-
isozyme HKI
3.8
-
D-glucose
-
30C, pH 7.5
4.7
-
D-glucose
-
-
5.5
-
D-glucose
-
hexokinase IV
8.4
8.5
D-glucose
P50521, Q09756
-
5
-
D-mannosamine
-
at 37C, pH 7.4
0.014
-
D-mannose
-
hexokinase III, at 30C, pH 8.1
0.01911
-
D-mannose
B8K2W7, -
pH 7.0, 22C
0.02164
-
D-mannose
B8K2W7, -
pH 7.6, 22C
0.02339
-
D-mannose
B8K2W7, -
pH 8.2, 22C
0.024
-
D-mannose
-
at 30C, pH 8.1
0.03
-
D-mannose
Q95PL2
recombinant TbHK1
0.03
-
D-mannose
Q3S2I3, -
30C, pH 8.0
0.038
-
D-mannose
-
HK3
0.04
-
D-mannose
-
glucokinase
0.043
-
D-mannose
Q7ZAH1, -
at 50C, pH 7.5
0.052
-
D-mannose
-
HK1
0.06
-
D-mannose
-
at 30C, pH 7.5
0.07
0.1
D-mannose
-
hexokinases Ia, Ib and Ic, at 37C, pH 7.2
0.07
-
D-mannose
P50521, Q09756
-
0.1
-
D-mannose
-
hexokinase Ia
0.1
-
D-mannose
-
at 37C, pH 8.1; hexokinase I
0.1
-
D-mannose
-
at 37C, pH 8.1
0.11
-
D-mannose
-
90C, pH 6.2
0.13
-
D-mannose
P50521, Q09756
-
0.13
-
D-mannose
-
pH 7.5, 50C, ATP as phosphoryl donor
0.149
-
D-mannose
-, Q6Q8A5
pH 8.4, 30C, recombinant isozyme hexokinase 2
0.15
-
D-mannose
-
hexokinase Ib
0.29
-
D-mannose
-
HK2
0.37
-
D-mannose
Q5SLJ4, -
pH 7.0, 50C
0.71
-
D-mannose
-
erythrocyte enzyme
0.85
-
D-mannose
-
-
1.03
-
D-mannose
-
recombinant HXK1, at 30C, pH 8
2
-
D-mannose
-
recombinant HXK2, at 30C, pH 8
4.6
-
D-mannose
-
30C, pH 7.5
0.231
-
GTP
Q3S2I3, -
30C, pH 8.0
0.654
-
GTP
B8K2W7, -
pH 8.2, 22C
0.717
-
GTP
B8K2W7, -
pH 7.0, 22C
0.788
-
GTP
B8K2W7, -
pH 7.6, 22C
1.9
-
ITP
-
MgITP2-, erythrocyte enzyme
2.5
-
ITP
-
hexokinase III, at 30C, pH 8.1
4.5
-
ITP
-
MgITP2-, hexokinase Ib
10
-
ITP
-
MgITP2-, at 37C, pH 8.1
12
-
ITP
-
MgITP2-, hexokinase Ia
16.6
-
ITP
-
MgITP2-, hexokinase I, at 37C, pH 8.1
0.56
-
MgATP2-
-
pH 8.0, 30C
0.67
-
MgATP2-
Q5W5U3
pH 7.2, 37C, recombinant full length enzyme
0.32
-
N-acetyl-D-glucosamine
-
pH 7.5, 50C, ATP as phosphoryl donor
41.6
-
N-acetyl-D-glucosamine
-
erythrocyte enzyme
0.231
-
TTP
Q3S2I3, -
30C, pH 8.0
1.162
-
UTP
B8K2W7, -
pH 7.0, 22C
1.598
-
UTP
B8K2W7, -
pH 7.6, 22C
1.791
-
UTP
B8K2W7, -
pH 8.2, 22C
2.2
-
UTP
Q3S2I3, -
30C, pH 8.0
5
-
UTP
-
MgUTP2-, hexokinase I, at 37C, pH 8.1
30
-
UTP
-
MgUTP2-, at 37C, pH 8.1
0.98
-
MgATP2-
Q5W5U3
pH 7.2, 37C, recombinant catalytic C-terminal domain
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
values for isoenzymes
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
of HXK1 mutants with modified active site
-
additional information
-
additional information
-
non-cooperative conditions shows an ordered, ternary-complex mechanism with MgADP- as the last product to be released, hyperbolic kinetics with both 2-deoxyglucose and MgATP2-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-, Q6Q8A5
kinetics of isozyme hexokinase 2
-
additional information
-
additional information
-
kinetics, mass spectrometry-based assay, overview, the Mg2+ concentration influence the kinetics
-
additional information
-
additional information
P33284
stopped-flow steady-state kinetics, dissociation constants of the monomer-homodimer equilibria
-
additional information
-
additional information
-
osmolytes decrease kcat/KM in the order of decreasing efficiency NaCl, urea, trimethylamine N-oxide/glycerol, betaine. For the organic osmolytes this order correlates with the degree of exclusion from protein/water interfaces; the osmolytes decreases kcat/KM in the order: NaCl/urea/trimethylamine-N-oxide dehydrate/glycerol/betaine. For the organic osmolytes this order correlates with the degree of exclusion from protein-water interfaces. Thus, the stronger the exclusion the weaker the perturbing effects on kcat/KM
-
additional information
-
additional information
-
kinetic parameters of hexokinase activity in wine yeast strains
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
29
-
2-deoxy-D-glucose
-
wild-type enzyme
2
3.7
ATP
-
37C, pH 7.4, mutant enzyme A456V
3.32
-
ATP
Q969A8, -
at 37C, pH 7
3.5
-
ATP
Q3S2I3, -
30C, pH 8.0
4.92
-
ATP
-
mutant enzyme V62E
6.42
-
ATP
-
mutant enzyme V62K
11
-
ATP
-
37C, pH 7.4, mutant enzyme K414E
14.9
-
ATP
-
mutant enzyme V62Q
25.7
-
ATP
-
mutant enzyme V62T
33.7
-
ATP
-
mutant enzyme V62F
43.1
-
ATP
-
mutant enzyme V62A
53.2
-
ATP
-
37C, pH 7.4, wild-type enzyme
53.6
-
ATP
-
mutant enzyme V62M
54
-
ATP
-
wild type enzyme, at 25C
59.9
-
ATP
-
mutant enzyme V62L
62.3
-
ATP
-
wild-type enzyme
84.9
-
ATP
-
37C, pH 7.4, mutant enzyme A456V
1.61
-
CTP
Q3S2I3, -
30C, pH 8.0
3.69
-
D-fructose
Q3S2I3, -
30C, pH 8.0
0.00091
-
D-glucose
-
mutant enzyme D205A, kcat less than 0.00091 s-1
0.18
-
D-glucose
-
truncated enzyme with removed helix alpha13
1.06
-
D-glucose
-
pH 7.5, 22C, soluble enzyme
1.67
-
D-glucose
-
pH 7.5, 22C, immobilized enzyme
2
3.7
D-glucose
-
37C, pH 7.4, mutant enzyme A456V
3.3
-
D-glucose
Q3S2I3, -
30C, pH 8.0
3.47
-
D-glucose
Q969A8, -
at 37C, pH 7
5.01
-
D-glucose
Q3S2I3, -
30C, pH 8.0
11
-
D-glucose
-
37C, pH 7.4, mutant enzyme K414E
17.4
-
D-glucose
-
mutant enzyme W167F, in 25 mM HEPES (pH 7.4), at 37C
24
-
D-glucose
-
mutant enzyme G72R, at 30C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
29
-
D-glucose
-
wild type enzyme
34
-
D-glucose
-
mutant enzyme G72R, at 37C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
37
-
D-glucose
-
glucokinase with C-terminal 5 alanine addition
38
-
D-glucose
-
wild-type enzyme
38
-
D-glucose
-
glucokinase with C-terminal 10 alanine addition
39
-
D-glucose
-
mutant enzyme Y214C
42.1
-
D-glucose
-
mutant enzyme W257F, in 25 mM HEPES (pH 7.4), at 37C
46.8
-
D-glucose
-
mutant enzyme W99F, in 25 mM HEPES (pH 7.4), at 37C
53.2
-
D-glucose
-
37C, pH 7.4, wild-type enzyme
54
-
D-glucose
-
mutant enzyme V62M, at 30C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
60.4
-
D-glucose
-
wild type enzyme, in 25 mM HEPES (pH 7.4), at 37C
61
-
D-glucose
-
mutant enzyme V62M, at 37C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
64
-
D-glucose
-
wild type enzyme, at 25C, in the presence of 0.02 mM activator N-[2-amino-4-fluoro-5-[(1-methyl-1H-imidazol-2-yl)sulfanyl]benzyl]-1,3-thiazol-2-amine
74
-
D-glucose
-
wild type enzyme, at 30C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
75
-
D-glucose
-
wild type enzyme, at 25C, in the presence of 0.02 mM activator LY-2121260
84.9
-
D-glucose
-
37C, pH 7.4, mutant enzyme A456V
101
-
D-glucose
-
wild type enzyme, at 37C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
195
-
D-glucose
-
recombinant HXK2, at 30C, pH 8
284
-
D-glucose
-
recombinant HXK1, at 30C, pH 8
483.3
-
D-glucose
Q95PL2
recombinant TbHK1
3.78
-
D-mannose
Q3S2I3, -
30C, pH 8.0
1.42
-
TTP
Q3S2I3, -
30C, pH 8.0
3.02
-
UTP
Q3S2I3, -
30C, pH 8.0
0.85
-
GTP
Q3S2I3, -
30C, pH 8.0
additional information
-
additional information
P19367
6000/min, wild-type and nonaggregating interface mutant hexokinase I
-
additional information
-
additional information
Q8ST54
natural hexokinase: 68160/min, recombinant hexokinase expressed in Escherichia coli XL-1 Blue: 18913/min, at pH 7.5
-
additional information
-
additional information
P33284
-
-
additional information
-
additional information
-
osmolytes decrease kcat/KM in the order ofedecreasing efficiency NaCl, urea, trimethylamine N-oxide/glycerol, betains. For the organic osmolytes this order correlates with the degree of exclusion from protein/water interfaces; the osmolytes decreases kcat/KM in the order: NaCl/urea/trimethylamine-N-oxide dehydrate/glycerol/betaine. For the organic osmolytes this order correlates with the degree of exclusion from protein-water interfaces. Thus, the stronger the exclusion the weaker the perturbing effects on kcat/KM
-
additional information
-
additional information
-
as the temperature is raised from 30C to 47.5C kcat decreases, falling to about 10 per sec (by 80%) at 50C
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic parameters of hexokinase activity in wine yeast strains
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
170
-
2-deoxy-D-glucose
-
pH 7.5, 50C
2416
259
-
ATP
-
pH 7.5, 50C
22040
52
-
CTP
-
pH 7.5, 50C
8829
1.4
-
D-fructose
-
pH 7.5, 50C
9137
247
-
D-glucosamine
-
pH 7.5, 50C
9197
717
-
D-glucose
-
pH 7.5, 50C
9202
420
-
D-mannose
-
pH 7.5, 50C
9286
100
-
N-acetyl-D-glucosamine
-
pH 7.5, 50C
13498
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
32.8
-
(2-pyridin-4-ylethane-1,1-diyl)bis(phosphonic acid)
-
against ATP, Kis
33.3
-
(2-pyridin-4-ylethane-1,1-diyl)bis(phosphonic acid)
-
against D-glucose, Kis
34.3
-
(2-pyridin-4-ylethane-1,1-diyl)bis(phosphonic acid)
-
Kii
36
-
(2-pyridin-4-ylethane-1,1-diyl)bis(phosphonic acid)
-
against D-glucose, Kii
0.0004
-
(3-bromo-phenyl)-aminomethylene-1,1-bisphosphonate
-
varied substrate is D-glucose, in the presence of 1 mM ATP and 3 mM MgCl2, Kis
0.0006
-
(3-bromo-phenyl)-aminomethylene-1,1-bisphosphonate
-
varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kis
0.0012
-
(3-bromo-phenyl)-aminomethylene-1,1-bisphosphonate
-
varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kii
0.0005
-
(9-ethyl-9H-3-carbazolyl)-aminomethylene-1,1-bisphosphonate
-
varied substrate is D-glucose, in the presence of 1 mM ATP and 3 mM MgCl2, Kis
0.0017
-
(9-ethyl-9H-3-carbazolyl)-aminomethylene-1,1-bisphosphonate
-
varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kis
0.0028
-
(9-ethyl-9H-3-carbazolyl)-aminomethylene-1,1-bisphosphonate
-
varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kii
0.01
0.02
1,5-Anhydro-D-glucitol 6-phosphate
-
catalytically active 51 kDa C fragment of hexokinase
0.0107
-
1,5-Anhydro-D-glucitol 6-phosphate
-
pH 8.0, mutant enzyme A464P/E465G
0.0108
-
1,5-Anhydro-D-glucitol 6-phosphate
-
pH 8.0, mutant enzyme Q466_H467insHMNLAEQ
0.014
-
1,5-Anhydro-D-glucitol 6-phosphate
P05708
recombinant wild-type hexokinase I
0.0164
-
1,5-Anhydro-D-glucitol 6-phosphate
-
pH 8.0, wild-type enzyme
0.018
-
1,5-Anhydro-D-glucitol 6-phosphate
P05708
recombinant D84E mutant hexokinase I
0.028
-
1,5-Anhydro-D-glucitol 6-phosphate
P05708
recombinant D84K mutant hexokinase I
0.033
-
1,5-Anhydro-D-glucitol 6-phosphate
P05708
recombinant D84A mutant hexokinase I
0.5
-
1,5-Anhydro-D-glucitol 6-phosphate
-
at pH 8.5
5
6
1,5-Anhydro-D-glucitol 6-phosphate
-
HK I+ and its D84A mutant
15
-
1,5-Anhydro-D-glucitol 6-phosphate
P19367
nonaggregating interface mutant hexokinase I, pH 7.8
16
-
1,5-Anhydro-D-glucitol 6-phosphate
-
HK I
23
-
1,5-Anhydro-D-glucitol 6-phosphate
P19367
wild-type hexokinase I, pH 7.8
32
-
1,5-Anhydro-D-glucitol 6-phosphate
-
D84A mutant of HK I
5
-
2,3-diphosphoglycerate
-
hexokinase III, at 30C, pH 7.2
14
-
2,3-diphosphoglycerate
-
at 30C, pH 8.1
0.0028
-
2-(pyridin-4-yl)-1-hydroxyethane-1,1-bisphosphonate
-
varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kis
0.0033
-
2-(pyridin-4-yl)-1-hydroxyethane-1,1-bisphosphonate
-
varied substrate is D-glucose, in the presence of 1 mM ATP and 3 mM MgCl2, Kis
0.0043
-
2-(pyridin-4-yl)-1-hydroxyethane-1,1-bisphosphonate
-
varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kii
0.006
-
2-(pyridin-4-yl)-1-hydroxyethane-1,1-bisphosphonate
-
varied substrate is D-glucose, in the presence of 1 mM ATP and 3 mM MgCl2, Kii
0.5
-
2-deoxy-D-glucose
P50521, Q09756
fructose as substrate
4
-
2-deoxy-D-glucose
P50521, Q09756
fructose as substrate
40.7
-
2-deoxy-D-glucose
-
pH 8.0, 30C, versus MgATP2-
13
-
2-phosphoglycerate
-
hexokinase III, at 30C, pH 7.2
14
-
2-phosphoglycerate
-
at 30C, pH 8.1
1.99
-
3-bromo-2-oxopropionic acid
-
-
12
-
3-phosphoglycerate
-
hexokinase III, at 30C, pH 7.2
21
-
3-phosphoglycerate
-
at 30C, pH 8.1
0.1
-
5-thio-D-glucose
-
inhibition of fructose phosphorylation, at 37C, pH 7.4
0.4
-
5-thio-D-glucose
-
-
50
-
6-deoxy-D-glucose
-
at 37C, pH 7.4
0.018
-
ADP
-
pH 7.5, 50C
0.03
-
ADP
-
non-cytosolic hexokinase from root; root, non-cytosolic enzyme
0.036
-
ADP
-
recombinant HXK1, at 30C, pH 8
0.04
-
ADP
-
HK1
0.04
-
ADP
O64390, Q9SQ76
; hexokinase 1
0.108
-
ADP
-
HK2
0.11
-
ADP
O64390, Q9SQ76
; hexokinase 2
0.122
-
ADP
-
pH 7.5, 22C, versus ATP, dependennt on Mg2+ concentration
0.193
-
ADP
-
recombinant HXK2, at 30C, pH 8
0.5
-
ADP
-
hexokinase III, at 30C, pH 7.2
0.55
-
ADP
-, Q56VN6
substrate glucose
0.723
-
ADP
-
inhibition with respect to ATP
1.3
-
ADP
Q8ST54
natural hexokinase from epimastigotes, at pH 7.5
1.5
-
ADP
-
competitive to ATP
1.5
-
ADP
-
versus MgATP2-, at 30C, pH 8.1
3.6
-
ADP
-
versus glucose, at 30C, pH 8.1
7
-
ADP
-
noncompetitive to glucose
0.00065
-
AMP
-
recombinant HXK1, at 30C, pH 8
0.031
-
AMP
-
recombinant HXK2, at 30C, pH 8
0.5
-
ATP
-
uncomplexed ATP4-, hexokinase III, at 30C, pH 7.2
1.5
-
ATP
-
uncomplexed ATP, erythrocyte enzyme, competitive to MgATP2-
3.6
-
ATP
-
at 30C, pH 8.1
0.15
-
citrate
-
-
4.5
-
Cr(III)-ATP
-
pH 6.9, 30C, versus MgATP2-
0.23
-
D-fructose
-
inhibition with respect to glucose
2.5
-
D-fructose 1,6-diphosphate
-
hexokinase III, at 30C, pH 7.2
4.6
-
D-fructose 1,6-diphosphate
-
at 30C, pH 8.1
0.5
-
D-fructose 6-phosphate
-
hexokinase III, at 30C, pH 7.2
0.88
-
D-fructose 6-phosphate
-
at 30C, pH 8.1
2.1
-
D-glucosamine
P50521, Q09756
fructose as substrate
11
-
D-glucosamine
P50521, Q09756
fructose as substrate
0.033
-
D-Glucose 1,6-bisphosphate
Q5W5U3
pH 7.2, 37C, recombinant catalytic C-terminal domain, versus MgATP2-
0.036
-
D-Glucose 1,6-bisphosphate
Q5W5U3
pH 7.2, 37C, recombinant full length enzyme, versus MgATP2-
3
-
D-Glucose 1,6-bisphosphate
-
-
0.04
-
D-glucose 1,6-diphosphate
-
hexokinase III, at 30C, pH 7.2
0.05
0.059
D-glucose 1,6-diphosphate
-
recombinant HK I, a truncate HK I form lacking the first 11 amino acids named HK-11aa, and the 50 kDa C-terminal half of HK I, at 37C, pH 7.2
0.127
-
D-glucose 1,6-diphosphate
-
at 30C, pH 8.1
21
22
D-glucose 1,6-diphosphate
-
hexokinase Ia, Ib and Ic, at 37C, pH 7.2
0.015
-
D-glucose 6-phosphate
-
ATP
0.02
-
D-glucose 6-phosphate
-
type I and type II isozymes
0.025
-
D-glucose 6-phosphate
-
-
0.026
-
D-glucose 6-phosphate
-
hexose
0.029
0.037
D-glucose 6-phosphate
-
recombinant HK I, a truncate HK I form lacking the first 11 amino acids named HK-11aa, and the 50 kDa C-terminal half of HK I, at 37C, pH 7.2
0.034
-
D-glucose 6-phosphate
-
at 30C, pH 8.1
0.045
-
D-glucose 6-phosphate
Q5W5U3
pH 7.2, 37C, recombinant full length enzyme
0.066
-
D-glucose 6-phosphate
Q5W5U3
pH 7.2, 37C, recombinant catalytic C-terminal domain
0.1
-
D-glucose 6-phosphate
-
type III isozyme
0.12
-
D-glucose 6-phosphate
-
hexokinase III, at 30C, pH 7.2
0.13
-
D-glucose 6-phosphate
-
catalytically active recombinant carboxyl-domain of hexokinase III, at 37C, pH 7.2
0.15
-
D-glucose 6-phosphate
-
at pH 8.5
0.18
-
D-glucose 6-phosphate
-
hexokinase C, versus ATP, at 0.2 mM glucose
0.226
-
D-glucose 6-phosphate
-
hexokinase III from lymphocytes, at 37C, pH 7.2
0.24
-
D-glucose 6-phosphate
-
wild type hexokinase II
0.43
-
D-glucose 6-phosphate
-
inhibition with respect to glucose
0.7
-
D-glucose 6-phosphate
-
inhibition with respect to ATP
1.4
-
D-glucose 6-phosphate
-
-
4
-
D-glucose 6-phosphate
O64390, Q9SQ76
pH 7, hexokinase 1
4.1
-
D-glucose 6-phosphate
-
HK1, at pH 7
0.06
-
D-mannose
-
glucokinase
0.85
-
D-xylose
-
glucokinase
25
-
D-xylose
-
hexokinase PI
80
-
D-xylose
-
hexokinase PII
2.5
-
dihydroxyacetonephosphate
-
hexokinase III, at 30C, pH 7.2
0.009
-
diphosphate
-, Q56VN6
-
0.035
-
diphosphate
-
inhibition with respect to ATP
0.5
-
diphosphate
Q8ST54
natural hexokinase from epimastigotes, at pH 7.5
0.7
-
diphosphate
Q8ST54
recombinant hexokinase expressed in Escherichia coli, at pH 7.5
0.4
-
glucose 1,6-disphosphate
-
IC50
13
15
glucose 6-phosphate
-
hexokinase Ia, Ib and Ic, at 37C, pH 7.2
0.5
-
mannoheptulose
-
non-cytoslic hexokinase from root; non-cytosolic enzyme
20
-
mannoheptulose
-
cytosolic enzyme; cytosolic hexokinase from root
9
-
Mg2+
-
erythrocyte enzyme, uncomplexed Mg2+
30
-
Mg2+
-
uncomplexed, hexokinase III, at 30C, pH 7.2
36
-
Mg2+
-
at 30C, pH 8.1
3
-
MgADP-
-
erythrocyte enzyme, mixed inhibitor versus MgATP2-
0.3
-
N-acetyl-D-glucosamine
-
-
0.7
-
N-acetyl-D-glucosamine
-
erythrocyte enzyme, competitive to glucose
0.63
-
N-acetylglucosamine
-
pH 8.0, 30C, versus 2-deoxyglucose
0.8
-
N-acetylglucosamine
-
pH 8.0, 30C, versus MgATP2-
50
-
N-acetylmannosamine
-
at 37C, pH 7.4
4.87
-
Ni2+
-
pH 7.6, 37C, versus ATP
9.97
-
Ni2+
-
pH 7.6, 37C, versus D-glucose
0.0035
-
palmitoyl-CoA
-
-
1.6
-
palmitoyl-CoA
-
-
5.3
-
phosphate
-
-
6
-
phosphate
-
catalytically active 51 kDa C fragment of hexokinase, versus ATP
7.8
-
phosphate
-
hexokinase III, at 30C, pH 7.2
13
-
phosphate
P05708
recombinant D84K mutant hexokinase I
15
-
phosphate
P05708
recombinant D84E mutant hexokinase I
17
-
phosphate
P05708
recombinant wild-type hexokinase I
17.9
-
phosphate
-
at 30C, pH 8.1
18
-
phosphate
P05708
recombinant D84A mutant hexokinase I
33
-
phosphate
-
recombinant HK I, a truncate HK I form lacking the first 11 amino acids named HK-11aa, and the 50 kDa C-terminal half of HK I, at 37C, pH 7.2
35
-
phosphate
-
intact hexokinase I
60
-
phosphate
-
catalytically active 51 kDa C fragment of hexokinase, versus glucose
8
-
phosphoenolpyruvate
-
hexokinase III, at 30C, pH 7.2
0.012
-
Trehalose 6-phosphate
-, Q96VP5
pH 7.5, 37C
3020
-
[[(3-bromophenyl)amino]methylene]bis(phosphonic acid)
-
against D-glucose, Kis
3021
-
[[(3-bromophenyl)amino]methylene]bis(phosphonic acid)
-
against ATP, Kii; against ATP, Kis
22
83
[[(9-ethyl-9H-carbazol-3-yl)amino]methylene]bis(phosphonic acid)
-
against ATP, Kii
2281
-
[[(9-ethyl-9H-carbazol-3-yl)amino]methylene]bis(phosphonic acid)
-
against D-glucose, Kis
2282
-
[[(9-ethyl-9H-carbazol-3-yl)amino]methylene]bis(phosphonic acid)
-
against ATP, Kis
7.8
-
MgADP-
-
erythrocyte enzyme, mixed inhibitor versus glucose
additional information
-
additional information
-
-
-
additional information
-
additional information
-
inhibition kinetics, overview
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.39
-
3-bromo-2-oxopropionic acid
-
-
4.2
-
ADP
-
pH 6.5, temperature not specified in the publication
10
-
ADP
-
pH 7.4, temperature not specified in the publication
0.0758
-
lauric acid
Q95PL2
IC50: 0.0758 mM, TbHK1
0.85
-
lonidamine
-
recombinant enzyme
0.0784
-
myristic acid
Q95PL2
IC50: 0.0784 mM, TbHK1
0.0624
-
palmitic acid
Q95PL2
IC50: 0.0624 mM, TbHK1
0.0045
-
Urea
-
frozen, pH 8.2, 25C
0.0053
-
Urea
-
control, pH 8.2, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.008
-
-
D-fructose as substrate, hxk mutant
0.033
0.04
-
-
0.06
-
-
HK3, at pH 8
0.076
-
-
D-glucose as substrate, hxk mutant
0.11
0.16
-
Hex I and II, at pH 8.2
0.114
-
-
healthy leaves, soluble glucokinase activity
0.151
-
-
D-glucose as substrate, wild type hexokinase
0.197
-
-
D-fructose as substrate, wild type hexokinase
0.199
-
-
TMV-infected leaves, soluble glucokinase activity
0.25
-
-
hexokinase type II, at 37C, pH 8.1
0.55
1.95
-
hexokinases Ia, Ib and Ic from adult erythrocytes, at 37C, pH 7.2
0.574
-
-
healthy leaves, particulate glucokinase activity
0.609
-
-
healthy leaves, soluble fructokinase activity
0.688
-
-
healthy leaves, particulate fructokinase activity; healthy leaves, total glucokinase activity
0.693
-
-
TMV-infected leaves, particulate glucokinase activity
0.72
-
-
HK2, at pH 8
0.786
-
A0SZU9
substrate: D-fructose
0.8
-
-
at 30C
0.84
-
-
HK1, at pH 8
0.892
-
-
TMV-infected leaves, total glucokinase activity
0.941
-
A0SZU9
substrate: D-mannose
1.297
-
-
healthy leaves, total fructokinase activity
1.43
2.22
-
hexokinases Ia, Ib and Ic from umbilical cord blood, at 37C, pH 7.2
1.44
-
Q5W5U3
cell extract of recombinant Escherichia coli expressing the full length enzyme
1.5
-
-
partially purified liver enzyme
1.95
-
A0SZU9
substrate: D-glucose
2
-
-
unpurified recombinant HK I and 50 kDa C-terminal half of HK I, at 22C
2
-
-
41C, pH 7.5
3.5
-
Q5W5U3
cell extract of recombinant Escherichia coli expressing the catalytic C-terminal domain of the enzyme
3.8
-
-
unpurified recombinant HK-11aa, a truncated HK I form lacking the first 11 amino acids, at 22C
4.04
-
Q969A8, -
recombinant hexokinase, expressed in Escherichia coli BL21, at 37C, pH 7
5.1
-
Trichosporonoides megachiliensis
-
-
5.3
-
Q3S2I3, -
-
5.6
-
-
in purified glycosomes, at 25C, pH 7.6
6
-
-
at 30 C
8.4
-
-
at 10 mM D-glucose
9.27
-
Q8ST54
recombinant hexokinase expressed in Escherichia coli XL-1 Blue, at 25C, pH 7.5
13.06
-
-
at 30 C, pH 8.1
15
-
-
D-fructose as substrate
19
-
-
D-mannose as substrate
19.3
-
B8K2W7, -
pH 7.6, 22C
19.44
-
Q8ST54
natural hexokinase from epimastigotes, at 25C, pH 7.5
20.25
-
-
at pH 7.2
22.2
-
-
at 25C, pH 7.2, hexokinase from erythrocytes
23.5
-
-
hexokinase C, at 30C, pH 7.5
26
-
-
pH 7.5, 50C, substrate: D-glucose
27
-
-
D-glucosamine as substrate
35
-
-
D-fructose
35
-
-
D-glucose as substrate
35.7
-
-
D-mannose as substrate
36
-
-
catalytically active recombinant carboxyl-domain of hexokinase type III, at 37C, pH 8.1
37
-
-
hexokinase from blood, at 25C
38.1
-
-
D-glucose as substrate
40
-
-
D-glucose
45
-
-
2-deoxy-D-glucose as substrate
58
-
-
hexokinase from heart, at 25C, pH 7.2
58.2
-
-
recombinant hexokinase I expressed in E. coli
60
61
P19367
wild-type and nonaggregating interface mutant hexokinase I, pH 7.8
60
-
-
enzyme form Hex C, at 25C, pH 8
60
-
-
intact 100 kDa enzyme
68
-
Q5SLJ4, -
pH 7.0, 50C
70
-
-
purified liver enzyme
86
-
-
hexokinase B, at 30C, pH 7.5
94
-
Q5W5U3
purified recombinant full length enzyme
95.7
-
-, Q96VP5
purified enzyme, substrate D-glucose
98.7
-
-
D-fructose as substrate
110
-
-
catalytically active 51 kDa C fragment of hexokinase
120
-
-
hexokinase type II, at 30C
120
-
-
commercial preparation
137
-
-
enzyme form Hex A, at 25C, pH 8
141
-
Q5W5U3
purified recombinant catalytic C-terminal domain of the enzyme
144
-
-
reticulocyte, hexokinase Ib, at 37C
144
-
-
pH 8.1; reticulocyte, hexokinase Ib, at 37C
144
-
-
purified recombinant HK I, at 22C
145.6
-
-
erythrocyte, at 37C
150
-
-
hexokinase from heart, at 25C, pH 8
155
-
-
reticulocyte, hexokinase Ia, at 37C
155
-
-
pH 8.1; reticulocyte, hexokinase Ia, at 37C
165
-
-
at 37C
180
-
-
purified recombinant HK-11aa, a truncated HK I form lacking the first 11 amino acids, at 22C
190
-
-
pure enzyme, at 25C, pH 7.6
191.5
-
-
hexokinase type III, at 37C, pH 8.1
192.5
-
-
at 37C
196
-
Q5RLG0, -
purified recombinant enzyme
268.8
-
-, Q96VP5
purified enzyme, substrate D-fructose
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
Q7ZAH1, -
-
additional information
-
-
the first 11 N-terminal amino acids influence the specific activity of HK
additional information
-
P05708
-
additional information
-
-
-
additional information
-
-, Q96VP5
activity in different strains, overview
additional information
-
-
activities at different substrate concentrations, overview
additional information
-
-, Q6Q8A5
-
additional information
-
-
-
additional information
-
P33284
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
optimal activity at pH 6.5 and 9.0 at 37C
7
-
Q969A8, -
-
7
-
Q5SLJ4, -
assay at
7.2
-
-
assay at
7.2
-
-
assay at
7.3
8.2
-
HK 1
7.4
8
-
-
7.4
-
-
assay at
7.4
-
-
assay at
7.4
-
P33284
assay at
7.4
-
-
assay at
7.5
8.2
-
isoenzyme Hex I
7.5
8.5
-
isoenzyme Hex II
7.5
8.8
Q8ST54
-
7.5
9
-
HK 2
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
Q7ZAH1, -
assay at
7.5
-
Q8ST54
assay at
7.5
-
Q5RLG0, -
-