Information on EC 2.7.1.3 - ketohexokinase

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

4933, 641283, 641285

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: role in formation of glycoaldehyde
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

758732, 759602

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Mammalia

641278

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

641282, 641275

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: conversion of fructose to glucose in liver homogenates involves the intermediary formation of D-fructose 1-phosphate
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: -
Products: -

ATP + D-ribose

Substrates: -
Products: -

ATP + D-ribose

Substrates: -
Products: -

ATP + D-sorbose

Substrates: -
Products: -

ATP + D-sorbose

Substrates: -
Products: -

ATP + D-tagatose

Substrates: -
Products: -

ATP + D-tagatose

Substrates: -
Products: -

ATP + D-xylose

ADP + D-xylose 1-phosphate

Substrates: -
Products: -

ATP + D-xylose

ADP + D-xylose 1-phosphate

Substrates: -
Products: -

ATP + D-xylulose

Substrates: -
Products: -

ATP + D-xylulose

4933, 641285

Substrates: -
Products: -

ATP + L-sorbose

Substrates: -
Products: -

ATP + L-sorbose

Substrates: specific for alpha anomer
Products: -

ATP + L-sorbose

Substrates: -
Products: -

additional information

Substrates: not: UTP
Products: -

additional information

Substrates: not: ITP
Products: -

additional information

Substrates: the minimum molecule for substrate activity seems to be (2R)-2-hydroxymethyl-3,4-dihydroxytetrahydrofuran
Products: -

additional information

Substrates: not: 2,6-anhydro-D-glucitol
Products: -

additional information

Substrates: specificity of fructokinase is for a tetrahydrofuran ring with beta-D-(or alpha-L-)configuration at position 2, L-configuration at position 3 and either D- or L-configuration at position 4 and 5
Products: -

additional information

Substrates: not: 2,6-anhydro-D-mannitol
Products: -

additional information

Substrates: not: 5-thio-D-fructose
Products: -

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

ATP + D-fructose

ADP + D-fructose 1-phosphate

15 entries

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

641276, 641281

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: D-fructose metabolism
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Haloarcula vallismortis ATCC 34679

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

ATP + D-fructose

ADP + D-fructose 1-phosphate

641283, 641285

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: role in formation of glycoaldehyde
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Mammalia

641278

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: conversion of fructose to glucose in liver homogenates involves the intermediary formation of D-fructose 1-phosphate
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: -
Products: -

ATP + D-fructose

ADP + D-fructose 1-phosphate

Substrates: -
Products: -

show all columns Go to Metals and Ions Search

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Cs+

CsCl

the enzyme is maximally active in the presence of 1.2 M KCl. Activity in the presence of RbCl and CsCl is similar to that observed in the presence of KCl

K+

5 entries

KCl

the enzyme is maximally active in the presence of 1.2 M KCl. Activity in the presence of RbCl and CsCl is similar to that observed in the presence of KCl

Li+

absolute requirement for both monovalent and divalent cations, when Mg2+ fills the requirement for divalent cation, K+ and Rb+ are the most active monovalent cations, NH4+, Na+, Cs+ and Li+ are decreasingly active

Mg2+

4 entries

Mn2+

inactive in absence of Mg2+ or Mn2+

Na+

NaCl

stimulates, yields 50% of the activity observed in equimolar KCl

NH4+

Rb+

RbCl

the enzyme is maximally active in the presence of 1.2 M KCl. Activity in the presence of RbCl and CsCl is similar to that observed in the presence of KCl

Tl+

activates

Cs+

Cs+

activates

K+

Km: 15 mM

K+

absolute requirement for both monovalent and divalent cations, when Mg2+ fills the requirement for divalent cation, K+ and Rb+ are the most active monovalent cations

K+

NH4+, Na+, Cs+ and Li+ are decreasingly active

K+

potassium acetate

K+

KCl activates

Mg2+

absolute requirement for both monovalent and divalent cations, for optimal activity the concentration of Mg2+ must equal or exceed the concentration of ATP

Mg2+

inactive in absence of Mg2+ or Mn2+

Mg2+

most active at a Mg2+ concentration of 1 mM. Mg2+ can not be replaced by Mn2+. ATP/Mg2+ in the ratio of 1:2 forms the actual substrate for ketohexokinase activity

Mg2+

show all columns Go to Inhibitor Search

641283, 641284, 641285

Na+

Na+

activates

NH4+

NH4+

activates

Rb+

Rb+

activates

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

1-deoxy-D-fructose

dead-end inhibitor

2,5-anhydro-D-glucitol

2,5-anhydro-D-lyxitol

2,5-anhydro-D-mannitol

2,5-anhydro-D-mannose

2,5-Anhydro-D-xylitol

2-(4-aminopiperidin-1-yl)-N8-(cyclopropylmethyl)-N4-(2-methylphenyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

2-ethyl-7-(3-hydroxy-3-methylpyrrolidin-1-yl)-5-(trifluoromethyl)-1H-pyrrolo[3,2-b]pyridine-6-carbonitrile

2-[(3R)-3-aminopiperidin-1-yl]-N8-(cyclopropylmethyl)-N4-[2-(methylsulfanyl)phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

2-[(3S)-3-aminopiperidin-1-yl]-N8-(cyclopropylmethyl)-N4-[2-(methylsulfanyl)phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

2-[3-(aminomethyl)azetidin-1-yl]-N8-(cyclopropylmethyl)-N4-[2-(methylsulfanyl)phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

2-[4-(aminomethyl)piperidin-1-yl]-N8-(cyclopropylmethyl)-N4-(2-methylphenyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

2-[4-(aminomethyl)piperidin-1-yl]-N8-(cyclopropylmethyl)-N4-[2-(methylsulfanyl)phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

3-(trifluoromethyl)quinoxalin-2(1H)-one

4,6-dimethyl-2-(morpholin-4-yl)pyridine-3-carbonitrile

4-chloromercuribenzoate

5-Thio-D-fructose

competitive to D-fructose

6-[(3S,4S)-3,4-dihydroxypyrrolidin-1-yl]-2-[(3S)-3-hydroxy-3-methylpyrrolidin-1-yl]-4-(trifluoromethyl)pyridine-3-carbonitrile

6-[4-(2-hydroxyethyl)piperazin-1-yl]-2-[(3S)-3-hydroxy-3-methylpyrrolidin-1-yl]-4-(trifluoromethyl)pyridine-3-carbonitrile

6-[4-(2-hydroxyethyl)piperazin-1-yl]-4-[3-(hydroxymethyl)piperidin-1-yl]-2-(trifluoromethyl)pyridine-3-carbonitrile

7-[(3R)-3-hydroxy-3-methylpyrrolidin-1-yl]-5-(trifluoromethyl)-1H-pyrrolo[3,2-b]pyridine-6-carbonitrile

7-[(3S)-3-hydroxy-3-methylpyrrolidin-1-yl]-5-(trifluoromethyl)-1H-pyrrolo[3,2-b]pyridine-6-carbonitrile

ADP

alpha-/gamma-mangostin

ATP

CrADP

dead-end inhibitor

cratoxyarborenone E

CrATP

dead-end inhibitor

D-Fructose 1-phosphate

competitive against D-fructose, noncompetitive to MgATP2-

D-mannoheptulose

D-psicose

D-ribono-gamma-lactone

D-ribose

D-sedoheptulose

D-tagatose

D-xylulose

DTNB

GDP

L-galactoheptulose

L-ribulose

L-sorbose

LiCl

methoxy-isobavachalcone

MgADP-

competitive to MgATP2-

N,N'-dicyclopropyl-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N-ethylmaleimide

N4-(2-bromophenyl)-N8-cyclopropyl-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N4-(2-chlorophenyl)-N8-cyclopropyl-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N4-(2-methylphenyl)-2-(piperazin-1-yl)-N8-(1,3-thiazol-2-ylmethyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N4-(2-methylphenyl)-2-(piperazin-1-yl)-N8-(prop-2-yn-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N4-(2-methylphenyl)-2-(piperazin-1-yl)-N8-(tetrahydrothiophen-2-ylmethyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N4-(2-methylphenyl)-2-(piperazin-1-yl)-N8-propylpyrimido[5,4-d]pyrimidine-4,8-diamine

N4-cyclohexyl-N8-cyclopropyl-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)-N8-(1,3-thiazol-2-ylmethyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)-N8-(pyridin-2-ylmethyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)-N8-(thiophen-2-ylmethyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-(2-cyclopropylethyl)-N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-(2-methoxyethyl)-N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-(cyclobutylmethyl)-N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-(cyclopropylmethyl)-2-(1,4-diazepan-1-yl)-N4-(2-methylphenyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-(cyclopropylmethyl)-2-(4-iminopiperidin-1-yl)-N4-(2-methylphenyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-(cyclopropylmethyl)-2-(4-methylpiperazin-1-yl)-N4-[2-(methylsulfanyl)phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-(cyclopropylmethyl)-2-[4-[(dimethylamino)methyl]piperidin-1-yl]-N4-[2-(methylsulfanyl)phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-(cyclopropylmethyl)-N2-methyl-N2-[2-(methylamino)ethyl]-N4-[2-(methylsulfanyl)phenyl]pyrimido[5,4-d]pyrimidine-2,4,8-triamine

N8-(cyclopropylmethyl)-N4-(2-methylphenyl)-2-(4-methylpiperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-(cyclopropylmethyl)-N4-(2-methylphenyl)-2-(morpholin-4-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-benzyl-N4-(2-methylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclohexyl-N4-(2-methylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclopropyl-2-(piperazin-1-yl)-N4-[2-(propan-2-yl)phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclopropyl-2-(piperazin-1-yl)-N4-[2-[(trifluoromethyl)sulfanyl]phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclopropyl-N4-(2-cyclopropylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclopropyl-N4-(2-ethoxyphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclopropyl-N4-(2-ethylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclopropyl-N4-(2-fluorophenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclopropyl-N4-(2-methoxyphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclopropyl-N4-(2-methylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclopropyl-N4-(3-methylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclopropyl-N4-phenyl-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclopropyl-N4-[2-(ethylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclopropyl-N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclopropyl-N4-[2-(methylsulfonyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclopropyl-N4-[3-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-cyclopropyl-N4-[4-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-ethyl-N4-(2-methylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-hexyl-N4-(2-methylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

N8-methyl-N4-(2-methylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

NH4Cl

osthole

PCMB

phloretin

Malus domestica extract, IC50 value 8.99.2 microg/mL

[(3R)-1-(5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-3-yl]methanol

additional information

6-[(3S,4S)-3,4-dihydroxypyrrolidin-1-yl]-2-[(3S)-3-hydroxy-3-methylpyrrolidin-1-yl]-4-(trifluoromethyl)pyridine-3-carbonitrile

nonbasic moderately potent and highly selective ketohexokinase inhibitor

6-[(3S,4S)-3,4-dihydroxypyrrolidin-1-yl]-2-[(3S)-3-hydroxy-3-methylpyrrolidin-1-yl]-4-(trifluoromethyl)pyridine-3-carbonitrile

nonbasic moderately potent and highly selective ketohexokinase inhibitor with favorable ADME and safety profiles and good exposure in rats

7-[(3S)-3-hydroxy-3-methylpyrrolidin-1-yl]-5-(trifluoromethyl)-1H-pyrrolo[3,2-b]pyridine-6-carbonitrile

7-[(3S)-3-hydroxy-3-methylpyrrolidin-1-yl]-5-(trifluoromethyl)-1H-pyrrolo[3,2-b]pyridine-6-carbonitrile

ADP

strong, noncompetitive

ADP

competitive

ADP

additional information

extracts of Angelica archangelica, Garcinia mangostana, Petroselinum crispum, and Scutellaria baicalensis exhibit ketohexokinase inhibitory activity and block fructose-induced ATP depletion and fructose-induced elevation in triglyerides and uric acid

additional information

not: glucose

additional information

the phosphorylation of D-fructose by ketohexokinase is resistant to inhibition by D-mannoheptulose

Go to Disease Search

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DISEASE

TITLE OF PUBLICATION

LINK TO PUBMED

Carcinogenesis

Prognostic Impact of Metabolism Reprogramming Markers Acetyl-CoA Synthetase 2 Phosphorylation and Ketohexokinase-A Expression in Non-Small-Cell Lung Carcinoma.

31750240

Carcinoma

KHK-A promotes the proliferation of oesophageal squamous cell carcinoma through the up-regulation of PRPS1.

32928708

Carcinoma

The expression of ketohexokinase is diminished in human clear cell type of renal cell carcinoma.

Carcinoma, Hepatocellular

A splicing switch from ketohexokinase-C to ketohexokinase-A drives hepatocellular carcinoma formation.

27088854

Carcinoma, Renal Cell

The expression of ketohexokinase is diminished in human clear cell type of renal cell carcinoma.

Cardiomegaly

HIF-driven SF3B1 induces KHK-C to enforce fructolysis and heart disease.

26083752

Diabetes Mellitus

Endogenous fructose is correlated with urinary albumin creatinine ratios and uric acid in type 2 diabetes mellitus.

34487756

Diabetes Mellitus, Type 2

Endogenous fructose is correlated with urinary albumin creatinine ratios and uric acid in type 2 diabetes mellitus.

34487756

Esophageal Squamous Cell Carcinoma

KHK-A promotes the proliferation of oesophageal squamous cell carcinoma through the up-regulation of PRPS1.

32928708

Fatty Liver

Divergent effects of glucose and fructose on hepatic lipogenesis and insulin signaling.

28972537

Fatty Liver

Ketohexokinase inhibition improves NASH by reducing fructose-induced steatosis and fibrogenesis.

33490936

Fructose Intolerance

Expression of rat liver ketohexokinase in yeast results in fructose intolerance.

8471037

Glioma

Ketohexokinase is involved in fructose utilization and promotes tumor progression in glioma.

30031605

Heart Diseases

HIF-driven SF3B1 induces KHK-C to enforce fructolysis and heart disease.

26083752

Hepatitis

Science letters: Proteomic analysis of differentially expressed proteins in mice with concanavalin A-induced hepatitis.

20205309

Hyperoxaluria

Calciuria, oxaluria and phosphaturia after ingestion of glucose, xylitol and sorbitol in two population groups with different stone-risk profiles.

19300989

Hypoglycemia

Ketohexokinase C blockade ameliorates fructose-induced metabolic dysfunction in fructose-sensitive mice.

29533924

Insulin Resistance

Fructose and hepatic insulin resistance.

31935149

ketohexokinase deficiency

Properties of normal and mutant recombinant human ketohexokinases and implications for the pathogenesis of essential fructosuria.

12941785

ketohexokinase deficiency

Tissue-Specific Fructose Metabolism in Obesity and Diabetes.

33057854

Liver Diseases

Fructose and fructose kinase in cancer and other pathologies.

34326012

Liver Diseases

Ketohexokinase inhibition improves NASH by reducing fructose-induced steatosis and fibrogenesis.

33490936

Metabolic Syndrome

Short-term fructose ingestion affects the brain independently from establishment of metabolic syndrome.

29017895

Neoplasms

Dietary fructose improves intestinal cell survival and nutrient absorption.

34408323

Neoplasms

Fructose and fructose kinase in cancer and other pathologies.

34326012

Neoplasms

Ketohexokinase is involved in fructose utilization and promotes tumor progression in glioma.

30031605

Neoplasms

KHK-A promotes the proliferation of oesophageal squamous cell carcinoma through the up-regulation of PRPS1.

32928708

Neoplasms

Prognostic Impact of Metabolism Reprogramming Markers Acetyl-CoA Synthetase 2 Phosphorylation and Ketohexokinase-A Expression in Non-Small-Cell Lung Carcinoma.

31750240

Neoplasms

The expression of ketohexokinase is diminished in human clear cell type of renal cell carcinoma.

Non-alcoholic Fatty Liver Disease

Ketohexokinase inhibition improves NASH by reducing fructose-induced steatosis and fibrogenesis.

33490936

Obesity

Inhibitors of Ketohexokinase: Discovery of Pyrimidinopyrimidines with Specific Substitution that Complements the ATP-Binding Site.

24900346

Obesity

Pyrimidinopyrimidine inhibitors of ketohexokinase: Exploring the ring C2 group that interacts with Asp-27B in the ligand binding pocket.

22795331

Proteinuria

IL-6/STAT3 signaling activation exacerbates high fructose-induced podocyte hypertrophy by ketohexokinase-A-mediated tristetraprolin down-regulation.

34252535

Entries 1 - 20 of 33

Show complete table

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2.9 - 47

2,5-anhydro-D-glucitol

10 - 67

2,5-anhydro-D-lyxitol

1.6 - 6.3

2,5-anhydro-D-mannitol

0.31 - 1.5

2,5-anhydro-D-mannose

1.2

5-keto-D-fructose

25°C, pH 7

0.15 - 3.3

ATP

10 entries

0.1 - 8.2

D-fructose

11 entries

120

D-mannoheptulose

25°C, pH 7

D-psicose

25°C, pH 7

D-ribono-gamma-lactone

25°C, pH 7

142 - 434

D-ribose

1.8 - 32.7

D-ribulose

2.2

D-sedoheptulose

25°C, pH 7

0.9

D-tagatose

0.44 - 1.4

D-xylose

D-xylulose

37°C, pH 7.5

1.53

GTP

pH 7.4

1.8

L-galacto-2-heptulose

25°C, pH 7, D-fructose 1-phosphate

0.37

L-ribulose

25°C, pH 7

0.4 - 19.3

L-sorbose

4 entries

2.9

2,5-anhydro-D-glucitol

25°C, pH 7

5.9

2,5-anhydro-D-glucitol

25°C, pH 7.5, MgATP2-2-: 4mM

2,5-anhydro-D-glucitol

25°C, pH 7.5, MgATP2-2-: 2mM

2,5-anhydro-D-lyxitol

25°C, pH 7

2,5-anhydro-D-lyxitol

25°C, pH 7.5, MgATP2-2-: 4mM

1.6

2,5-anhydro-D-mannitol

25°C, pH 7

1.7

2,5-anhydro-D-mannitol

25°C, pH 7.5, MgATP2-2-: 4mM

6.3

2,5-anhydro-D-mannitol

25°C, pH 7.5, MgATP2-2-: 2mM

0.31

2,5-anhydro-D-mannose

25°C, pH 7.5, MgATP2-: 2mM

2,5-anhydro-D-mannose

25°C, pH 7

1.5

2,5-anhydro-D-mannose

25°C, pH 7.5, MgATP2-: 4mM

0.15

ATP

25°C, pH 7, ketohexokinase-C wild type

0.15

ATP

ATP in form of MgATP2-

0.32

ATP

25°C, pH 7, ketohexokinase-C A43T

0.32

ATP

ATP in form of MgATP2-

0.36

ATP

25°C, pH 7, ketohexokinase-A wild type

0.36

ATP

ATP in form of MgATP2-

0.41

ATP

25°C, pH 7, ketohexokinase-A A43T

0.41

ATP

ATP in form of MgATP2-

1.43

ATP

pH 7.4

3.3

ATP

pH 9.0, 37°C

0.1

D-fructose

25°C, pH 7

0.5

D-fructose

0.5

D-fructose

25°C, pH 7.5, MgATP2-: 4mM

0.56

D-fructose

pH 7.4, cosubstrate GTP

0.8

D-fructose

25°C, pH 7, ketohexokinase-C wild type

0.83

D-fructose

pH 7.4, + ATP

0.84

D-fructose

25°C, pH 7, ketohexokinase-C A43T

0.86

D-fructose

37°C, pH 7.5

D-fructose

pH 9.0, 37°C

D-fructose

25°C, pH 7, ketohexokinase-A wild type

8.2

D-fructose

25°C, pH 7, ketohexokinase-A A43T

142

D-ribose

25°C, pH 7

201

D-ribose

25°C, pH 7, ketohexokinase-A wild type

434

D-ribose

25°C, pH 7, ketohexokinase-C wild type

1.8

D-ribulose

25°C, pH 7, ketohexokinase-C wild type

32.7

D-ribulose

25°C, pH 7, ketohexokinase-A wild type

0.9

D-tagatose

25°C, pH 7

0.9

D-tagatose

25°C, pH 7.5, MgATP2-: 4mM

0.44

D-xylose

25°C, pH 7, ketohexokinase-C wild type

D-xylose

25°C, pH 7, ketohexokinase-A wild type

1.4

D-xylose

25°C, pH 7

0.4

L-sorbose

25°C, pH 7.5, MgATP2-: 4mM

0.43

L-sorbose

25°C, pH 7

5.8

L-sorbose

25°C, pH 7, ketohexokinase-C wild type

19.3

L-sorbose

25°C, pH 7, ketohexokinase-A wild type

show all columns Go to Turnover Number Search

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

1.7 - 7.6

D-fructose

4 entries

1.55 - 8.2

D-ribose

4.8 - 7.6

D-ribulose

7.6 - 11.1

D-xylulose

5.2 - 6.5

L-sorbose

1.7

D-fructose

25°C, pH 7, C-A43T

5.9

D-fructose

25°C, pH 7, A-A43T

6.9

D-fructose

25°C, pH 7, ketohexokinase-A

7.6

D-fructose

25°C, pH 7, ketohexokinase-C

1.55

D-ribose

25°C, pH 7, ketohexokinase-A

8.2

D-ribose

25°C, pH 7, ketohexokinase-C

4.8

D-ribulose

25°C, pH 7, ketohexokinase-C

7.6

D-ribulose

25°C, pH 7, ketohexokinase-A

7.6

D-xylulose

25°C, pH 7, ketohexokinase-C

11.1

D-xylulose

25°C, pH 7, ketohexokinase-A

5.2

L-sorbose

25°C, pH 7, ketohexokinase-C

6.5

L-sorbose

25°C, pH 7, ketohexokinase-C

show all columns Go to Ki Value Search

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Ki VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.1 - 0.2

ADP

0.1

ADP

pH 9.0, 37°C

0.2

ADP

pH 7.5, 37°C

show all columns Go to IC50 Value Search

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IC50 VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.0002

2-(4-aminopiperidin-1-yl)-N8-(cyclopropylmethyl)-N4-(2-methylphenyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00148

2-ethyl-7-(3-hydroxy-3-methylpyrrolidin-1-yl)-5-(trifluoromethyl)-1H-pyrrolo[3,2-b]pyridine-6-carbonitrile

Homo sapiens

23°C, pH 7.4

0.000018

2-[(3R)-3-aminopiperidin-1-yl]-N8-(cyclopropylmethyl)-N4-[2-(methylsulfanyl)phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.000023

2-[(3S)-3-aminopiperidin-1-yl]-N8-(cyclopropylmethyl)-N4-[2-(methylsulfanyl)phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00003

2-[3-(aminomethyl)azetidin-1-yl]-N8-(cyclopropylmethyl)-N4-[2-(methylsulfanyl)phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00007

2-[4-(aminomethyl)piperidin-1-yl]-N8-(cyclopropylmethyl)-N4-(2-methylphenyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00001

2-[4-(aminomethyl)piperidin-1-yl]-N8-(cyclopropylmethyl)-N4-[2-(methylsulfanyl)phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.1

3-(trifluoromethyl)quinoxalin-2(1H)-one

Homo sapiens

23°C, pH 7.4

0.319

4,6-dimethyl-2-(morpholin-4-yl)pyridine-3-carbonitrile

Homo sapiens

23°C, pH 7.4

0.00039 - 0.00045

6-[(3S,4S)-3,4-dihydroxypyrrolidin-1-yl]-2-[(3S)-3-hydroxy-3-methylpyrrolidin-1-yl]-4-(trifluoromethyl)pyridine-3-carbonitrile

0.00103

6-[4-(2-hydroxyethyl)piperazin-1-yl]-2-[(3S)-3-hydroxy-3-methylpyrrolidin-1-yl]-4-(trifluoromethyl)pyridine-3-carbonitrile

Homo sapiens

23°C, pH 7.4

0.01679

6-[4-(2-hydroxyethyl)piperazin-1-yl]-4-[3-(hydroxymethyl)piperidin-1-yl]-2-(trifluoromethyl)pyridine-3-carbonitrile

Homo sapiens

23°C, pH 7.4

0.02421

7-[(3R)-3-hydroxy-3-methylpyrrolidin-1-yl]-5-(trifluoromethyl)-1H-pyrrolo[3,2-b]pyridine-6-carbonitrile

Homo sapiens

23°C, pH 7.4

0.00064 - 0.00067

7-[(3S)-3-hydroxy-3-methylpyrrolidin-1-yl]-5-(trifluoromethyl)-1H-pyrrolo[3,2-b]pyridine-6-carbonitrile

0.0015

alpha-/gamma-mangostin

Homo sapiens

37°C, pH 7.2

0.001

cratoxyarborenone E

Homo sapiens

37°C, pH 7.2

0.0002

methoxy-isobavachalcone

Homo sapiens

37°C, pH 7.2

0.009

N,N'-dicyclopropyl-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00017

N4-(2-bromophenyl)-N8-cyclopropyl-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00054

N4-(2-chlorophenyl)-N8-cyclopropyl-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00006

N4-(2-methylphenyl)-2-(piperazin-1-yl)-N8-(1,3-thiazol-2-ylmethyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0017

N4-(2-methylphenyl)-2-(piperazin-1-yl)-N8-(prop-2-yn-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0003

N4-(2-methylphenyl)-2-(piperazin-1-yl)-N8-(tetrahydrothiophen-2-ylmethyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0004

N4-(2-methylphenyl)-2-(piperazin-1-yl)-N8-propylpyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.009

N4-cyclohexyl-N8-cyclopropyl-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.000016

N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)-N8-(1,3-thiazol-2-ylmethyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0000098

N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)-N8-(pyridin-2-ylmethyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00003

N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)-N8-(thiophen-2-ylmethyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0000071

N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00005

N8-(2-cyclopropylethyl)-N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.000007

N8-(2-methoxyethyl)-N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.000018

N8-(cyclobutylmethyl)-N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0003

N8-(cyclopropylmethyl)-2-(1,4-diazepan-1-yl)-N4-(2-methylphenyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00071

N8-(cyclopropylmethyl)-2-(4-iminopiperidin-1-yl)-N4-(2-methylphenyl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00011

N8-(cyclopropylmethyl)-2-(4-methylpiperazin-1-yl)-N4-[2-(methylsulfanyl)phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00014

N8-(cyclopropylmethyl)-2-[4-[(dimethylamino)methyl]piperidin-1-yl]-N4-[2-(methylsulfanyl)phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00013

N8-(cyclopropylmethyl)-N2-methyl-N2-[2-(methylamino)ethyl]-N4-[2-(methylsulfanyl)phenyl]pyrimido[5,4-d]pyrimidine-2,4,8-triamine

Homo sapiens

pH and temperature not specified in the publication

0.0015

N8-(cyclopropylmethyl)-N4-(2-methylphenyl)-2-(4-methylpiperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.007

N8-(cyclopropylmethyl)-N4-(2-methylphenyl)-2-(morpholin-4-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0003

N8-benzyl-N4-(2-methylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0016

N8-cyclohexyl-N4-(2-methylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.005

N8-cyclopropyl-2-(piperazin-1-yl)-N4-[2-(propan-2-yl)phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.003

N8-cyclopropyl-2-(piperazin-1-yl)-N4-[2-[(trifluoromethyl)sulfanyl]phenyl]pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00038

N8-cyclopropyl-N4-(2-cyclopropylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0002

N8-cyclopropyl-N4-(2-ethoxyphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00013

N8-cyclopropyl-N4-(2-ethylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0015

N8-cyclopropyl-N4-(2-fluorophenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0001

N8-cyclopropyl-N4-(2-methoxyphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.00021

N8-cyclopropyl-N4-(2-methylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0028

N8-cyclopropyl-N4-(3-methylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0032

N8-cyclopropyl-N4-phenyl-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.009

N8-cyclopropyl-N4-[2-(ethylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.000012

N8-cyclopropyl-N4-[2-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.009

N8-cyclopropyl-N4-[2-(methylsulfonyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.002

N8-cyclopropyl-N4-[3-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.009

N8-cyclopropyl-N4-[4-(methylsulfanyl)phenyl]-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0023

N8-ethyl-N4-(2-methylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0004

N8-hexyl-N4-(2-methylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0004

N8-methyl-N4-(2-methylphenyl)-2-(piperazin-1-yl)pyrimido[5,4-d]pyrimidine-4,8-diamine

Homo sapiens

pH and temperature not specified in the publication

0.0007

osthole

Homo sapiens

37°C, pH 7.2

0.118

[(3R)-1-(5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-3-yl]methanol

Homo sapiens

23°C, pH 7.4

0.00039

6-[(3S,4S)-3,4-dihydroxypyrrolidin-1-yl]-2-[(3S)-3-hydroxy-3-methylpyrrolidin-1-yl]-4-(trifluoromethyl)pyridine-3-carbonitrile

Homo sapiens

23°C, pH 7.4, splice variant KHK-A

0.00045

6-[(3S,4S)-3,4-dihydroxypyrrolidin-1-yl]-2-[(3S)-3-hydroxy-3-methylpyrrolidin-1-yl]-4-(trifluoromethyl)pyridine-3-carbonitrile

Homo sapiens

23°C, pH 7.4, splice variant KHK-C

0.00064

7-[(3S)-3-hydroxy-3-methylpyrrolidin-1-yl]-5-(trifluoromethyl)-1H-pyrrolo[3,2-b]pyridine-6-carbonitrile

Rattus norvegicus

23°C, pH 7.4

0.00067

7-[(3S)-3-hydroxy-3-methylpyrrolidin-1-yl]-5-(trifluoromethyl)-1H-pyrrolo[3,2-b]pyridine-6-carbonitrile

Homo sapiens

23°C, pH 7.4

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.00014

in B and non-B cells. The reaction velocity is recorded in the presence of D-fructose (1.0 mM) and K+ in heated homogenate, it is expressed relative to protein content.

0.000158

in parotid gland. The reaction velocity is recorded in the presence of D-fructose (1.0 mM) and K+ in heated homogenate, it is expressed relative to protein content.

0.00046

in islets. The reaction velocity is recorded in the presence of D-fructose (1.0 mM) and K+ in heated homogenate, it is expressed relative to protein content.

0.00082

in pancreas. The reaction velocity is recorded in the presence of D-fructose (1.0 mM) and K+ in heated homogenate, it is expressed relative to protein content.

0.00245

in ileum. The reaction velocity is recorded in the presence of D-fructose (1.0 mM) and K+ in heated homogenate, it is expressed relative to protein content.

0.02154

in liver. The reaction velocity is recorded in the presence of D-fructose (1.0 mM) and K+ in heated homogenate, it is expressed relative to protein content.

9.4

additional information

enzyme activities in transgenic plants of Solanum tuberosum

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5.5 - 7.8

assay at

7.4

assay at

assay at

show all columns Go to pH Range Search

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5.1 - 9.1

pH 5.1: about 20% of activity maximum, pH 9.1: about 30% of activity maximum

7.5 - 10.5

activity increases about twofold from pH 7.5 to pH 10.5

show all columns Go to Temperature Optimum Search

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

show all columns Go to Temperature Range Search

assay at

assay at

assay at

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TEMPERATURE RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

heat resistant

show all columns Go to Pi Value Search

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pI VALUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5.6

2-D gel analysis

5.7

5.7

isoelectric focusing, LKB (pH 3-10) ampholytes were used with 7.5% polyacrylamide gels

5.7

calculated from amino acid sequence

682791

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

641276, 641277, 641279, 641281

brenda

706706

brenda

Haloarcula vallismortis ATCC 34679

brenda

brenda

brenda

brenda

brenda

brenda

4933, 641283, 641284, 641285, 678985

brenda

682791, 701467

SwissProt

brenda

brenda

SwissProt

brenda

737995, 739133, 739450

brenda

758732, 759602, 760221

SwissProt

brenda

brenda

SwissProt

brenda

641275, 641282, 660306

brenda

SwissProt

brenda

adult albino Wistar rats of both sexes

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

bone

relatively low expression of ketohexokinase.The expression profile for ketohexokinase in human is derived from from Unigene by adding the number of EST clones obtained from normal tissues

brenda

relatively low expression of ketohexokinase.The expression profile for ketohexokinase in human is derived from from Unigene by adding the number of EST clones obtained from normal tissues

brenda

chorion

ketohexokinase protein is detected in the trophectoderm at day 11 of pregnancy

brenda

expressed at significantly higher level in glioma tissues than in non-tumor brain

brenda

brenda

brenda

hepatocellular carcinoma cell

739133

brenda

ileum

renal cell carcinoma cell

12.4% of the phosphorylation of D-fructose by ileum homogenates is attributable to ketohexokinase

brenda

relatively high expression of ketohexokinase.The expression profile for ketohexokinase in human is derived from from Unigene by adding the number of EST clones obtained from normal tissues

brenda

brenda

represent the most prevalent cancer of the kidney. The mean ketohexokinase activity in the renal cell carcinoma tissue samples is approximately 1.4fold lower than that in their normal kidney tissue. Ketohexokinase activity is approximately 1.5fold lower in pT3 renal cell carcinoma tissue than that in pT1 renal cell carcinoma tissue. The enzyme activity of tumor in histological grade 3 is 1.8fold lower than for grade 1 tumor(reaction mixture activity assay: acid-treated supernatant (100 microl) containing 10 mM MgCl2, 50 mM TrisHCl, pH 7.4, 10 mM ATP, 50 mM N-acetyl-D-glucosamine, 10 mM D[UL-14C]fructose and water, at 37°C). The expression level of ketohexokinase mRNA is reduced two- to eightfold in nearly all the clear cell renal cell carcinoma tissue samples compared with normal kidney, except for one renal cell carcinoma sample.

brenda

brenda

relatively low expression of ketohexokinase.The expression profile for ketohexokinase in human is derived from from Unigene by adding the number of EST clones obtained from normal tissues

brenda

brenda

ketohexokinase protein is detected at all stages of gestation studied through day 85

brenda

uterine endometrium

expression of ketohexokinase mRNA is greater from day 9 through 17 of pregnancy compared to the corresponding days of the estrous cycle. There is an increase in expression of KHK mRNA through day 85, with peaks at days 30 and 85. Ketohexokinase protein is only detectable in GE of the endometrium at day 30 of pregnancy

brenda

additional information

5 entries

brain

brenda

brenda

relatively high expression of ketohexokinase.The expression profile for ketohexokinase in human is derived from from Unigene by adding the number of EST clones obtained from normal tissues

brenda

expressed at significantly higher level in glioma tissues than in non-tumor brain

brenda

brain

Mus musculus

the expression of ketohexokinase is investigated in coronal sections of the hindbrain containing the cerebellum. There is a lack of general DIG-labeled cells in the molecular layer of the cerebellum, but the Purkinje cell layer, which separates the molecular layer from the granular layer, demonstrated the strongest DIG labeling. DIG-labeled RNA in situ hybridization identifies specific cellular location of ketohexokinase mRNA expression.

brenda

heart

brenda

brenda

relatively low expression of ketohexokinase.The expression profile for ketohexokinase in human is derived from from Unigene by adding the number of EST clones obtained from normal tissues

brenda

brenda

brenda

high expression of ketohexokinase.The expression profile for ketohexokinase in human is derived from from Unigene by adding the number of EST clones obtained from normal tissues

brenda

liver

641276, 641277, 641279, 641281

brenda

brenda

brenda

brenda

high expression of ketohexokinase.The expression profile for ketohexokinase in human is derived from from Unigene by adding the number of EST clones obtained from normal tissues

brenda

brenda

brenda

brenda

641275, 641282, 660306

brenda

liver

the phosphorylation of D-fructose by liver homogenates is attributable to ketohexokinase

brenda

brenda

relatively low expression of ketohexokinase.The expression profile for ketohexokinase in human is derived from from Unigene by adding the number of EST clones obtained from normal tissues

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of the intestine

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relatively low expression of ketohexokinase.The expression profile for ketohexokinase in human is derived from from Unigene by adding the number of EST clones obtained from normal tissues

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pancreas

activity of ketohexokinase in pancreas homogenates. In pancreatic islets ketohexokinase activity is present.

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placenta

relatively low expression of ketohexokinase.The expression profile for ketohexokinase in human is derived from from Unigene by adding the number of EST clones obtained from normal tissues

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placenta

expression of ketohexokinase mRNA increases from day 30 to 40 of pregnancy

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ketohexokinase-dependent induction by fructose of lipogenic gene expression

759645

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additional information

not expressed in lung

706706

brenda

additional information

peripheral isoform (isoform C is a hepatic isoform)

brenda

additional information

peripheral isoform (isoform C is a hepatic isoform)

brenda

additional information

there is no biologically significant amount of ketohexokinase in the parotid gland

brenda

additional information

semi-purified B and non-B islet cells are investigated. The major fraction of D-fructose phosphorylation by islet cell homogenates (B and non-B) is not attributable to ketohexokinase.

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Highest Expressing Human Cell Lines

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

drug target

ketohexokinase may be a therapeutic target. Complete knockout of all ketohexokinase isoforms prevents fructose-induced disease. In contrast, selective knockout of the ubiquitous, low-activity KHK-A isoform exacerbates fructose-induced disease, possibly by increasing flux through the KHK-C isoform expressed in key metabolic tissues, like liver

malfunction

metabolism

malfunction

two mouse knockout models are generated: one strain is selectively deficient in peripheral Khk-A, while the second strain lacks activity of both Khk-A and Khk-C. Both homozygous knockout mice are healthy and fertile and display minimal biochemical abnormalities under basal dietary conditions

723348

malfunction

functionally, knockdown of ketohexokinase can significantly inhibit cell proliferation and migration of glioma cells in fructose medium

metabolism

fructose-driven glycolytic respiration in Heterocephalus glaber tissues avoids feedback inhibition of glycolysis via phosphofructokinase, allowing continued glycolytic flux independent of cellular energy status and supporting viability

metabolism

key enzyme involved in fructose catabolism

metabolism

ketohexokinase overexpression is significantly correlated with tumor malignancy and poor survival of glioma patients

metabolism

increased fructose consumption and its subsequent metabolism are implicated in hepatic steatosis, dyslipidemia, obesity, and insulin resistance

metabolism

Mus musculus

P97328

ketohexokinase-dependent induction by fructose of lipogenic gene expression in small intestine

759645

metabolism

Mus musculus

P97328

fructose metabolism by ketohexokinase increases sodium hydrogen exchanger activity in renal proximal tubular cells via decreased intracellular cAMP level, resulting in increased renal sodium reabsorption and blood pressure in mice

759646

metabolism

fructose increases de novo lipogenesis through the efficient and uninhibited action of ketohexokinase and aldolase B, which yields substrates for fatty-acid synthesis. Chronic fructose consumption further enhances the capacity for hepatic fructose metabolism via activation of several key transcription factors (i.e. SREBP1c and ChREBP), which augment expression of lipogenic enzymes, increasing lipogenesis, further compounding hypertriglyceridemia, and hepatic steatosis. Hepatic insulin resistance develops from diacylglycerol-PKCe mediated impairment of insulin signaling and possibly additional mechanisms

760221

metabolism

increased fructose consumption and its subsequent metabolism are implicated in hepatic steatosis, dyslipidemia, obesity, and insulin resistance

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

Show AA Sequence and Transmembrane Helices (707 entries)
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PDB

SCOP

CATH

UNIPROT

ORGANISM

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

100000

sucrose density gradient sedimentation analysis

29000

2 * 29000 SDS-PAGE in the presence of dithiothreitol

32730

33000

? * 33000, immunoblot

39000

2 * 39000, SDS-PAGE

56000

gel filtration, ultracentrifugation

75000

gel filtration

95500

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gel filtration

32730

2-D gel analysis

32730

theoretical

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

? * 33000, immunoblot

dimer

homodimer

gel filtration, nondenaturing PAGE

dimer

Go to Crystallization (commentary) Search

2 * 29000 SDS-PAGE in the presence of dithiothreitol

dimer

2 * 39000, SDS-PAGE

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

show all columns Go to Protein Variants Search

at 20°C, 10 mg/ml protein pH 7.5 in 10 mM HEPES, vapour-diffusion method applied in hanging- and sitting-drop variants, protein desalted and with Centricon-10 concentrated, precipitants: 2-propanol and MPD, space group: P212121 or P21212 with a: 93.4, b: 121.5 and c: 108.4 A

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

A43T

decreased thermostability of ketohexokinase-A and ketohexokinase-C

G40R

both ketohexokinase-A and ketohexokinase-C become inactive and largely unsoluble

additional information

heterologous expression of the enzyme in potato plants, showing elevated activity in leaves and tubers, leads to inhibited rates of photosynthesis, severe growth retardation and abnormal leaf development, phenotype analysis

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

25°C, 2 h, totally inactivated in 0.1 M KCl/50 mM Tris-HCl (pH 9.0). Stabilizing effect of KCl increases with increasing KCl concentration between 0.1 and 2.5 M (ranging from 30 to 98% of the total). Addition of 50 mM phosphate aids in stabilization of ketohexokinase activity in 0.1 M KCI for about 24 h. Although it is inhibitory for expression of ketohexokinase activity, (NH4)2SO4 stabilizes

C-A43T rapidly loss in activity in absence of glycerol

30 min ketohexokinase-A little loss in activity, ketohexokinase-C completely inactivated

30 min, 5% loss of activity

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

(NH4)2SO4 stabilizes

stabilizing effect of KCl increases with increasing KCl concentration between 0.1 and 2.5 M (ranging from 30 to 98% of the total)

Go to Storage Stability Search

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STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

-20°C

-20°C, stable for several months

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

7 entries

641277, 641279

Go to Cloned (commentary) Search

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

737995

construction of transgenic Solanum tuberosum plants expressing the enzyme under control of the CaMV 35S promotor by Agrobacterium tumefaciens infection system

expressed in Escherichia coli

expression in Escherichia coli

overexpression in Escherichia coli

expression in Escherichia coli

show all columns Go to Application Search

expression in Escherichia coli

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

analysis

development of a three-dimensional chemical-feature-based QSAR pharmacophore model by using Discovery Studio v2.5 to identify inhibitors, and screening of chemical databases for validated pharmacophore hypothesis. Hit compounds show good hydrogen bonding interactions with the keyamino acids such as Arg108, Asp258, Gly41, Gly255, Asn42 and water molecules W12, W27, respectively

737891

medicine

medicine

compared with normal hepatocytes, hepatocellular carcinoma cells markedly reduce the rate of fructose metabolism and the level of reactive oxygen species, as a result of a c-Myc-dependent and heterogeneous nuclear ribonucleoprotein H1- and H2-mediated switch from expression of the high-activity fructokinase KHK-C to the low-activity KHK-A isoform. KHK-A acts as a protein kinase, phosphorylating and activating phosphoribosyl pyrophosphate synthetase PRPS1. c-Myc, hnRNPH1/2 and KHK-A expression levels and PRPS1 Thr225 phosphorylation levels correlate with each other in hepatocellular carcinoma specimens and are associated with poor prognosis for hepatocellular carcinoma

739133

medicine

top print hide References Search

mutually exclusive splicing of adjacent exons 3A and 3C in ketohexokinase precursor RNA results in expression of ketohexokinase isoform KHK-A or KHK-C. KHK-A but not KHK-C interacts with phosphoribosyl diphosphate synthetase PRPS1. KHK-A functions as a protein kinase and directly phosphorylates PRPS1 at T225. This phosphorylation blocks the binding of the allosteric inhibitor ADP to PRPS1, thereby abrogating the feedback inhibition by ADP and leading to elevated de novo nucleic acid synthesis by constitutively activating PRPS1 in hepytocellular carcinoma cells

737995

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Bais, R.; James, H.M.; Rofe, A.M.; Conyers, A.J.

The purification and properties of human liver ketohexokinase. A role for ketohexokinase and fructose-bisphosphate aldolase in the metabolic production of oxalate from xylitol

Biochem. J.

230

53-60

1985

Homo sapiens

2996495

brenda

Cori, G.T.; Ochoa, S.; Slein, M.W.; Cori, C.F.

The metabolism of fructose in liver. Isolation of fructose-I-phosphate and inorganic pyrophosphate

Biochim. Biophys. Acta

304-317

1951

Rattus norvegicus

14858418

brenda

Hers, H.G.

La fructokinase du foie

Biochim. Biophys. Acta

416-423

1952

Bos taurus

brenda

Parks, R.E.; Ben-Gershom, E.; Lardy, H.E.

Liver fructokinase

J. Biol. Chem.

227

231-242

1957

Bos taurus

13449068

brenda

641278

Weiser, M.M.; Quill, H.

Estimation of fructokinase (ketohexokinase) in crude tissue preparations

Methods Enzymol.

41B

61-63

1975

Mammalia

brenda

Raushel, F.M.; Cleland, W.W.

Bovine liver fructokinase: purification and kinetic properties

Biochemistry

2169-2175

1977

Bos taurus

193556

brenda

Raushel, F.M.; Cleland, W.W.

The substrate and anomeric specificity of fructokinase

J. Biol. Chem.

248

8174-8177

1973

Bos taurus, Saccharomyces cerevisiae

4356621

brenda

Phillips, M.I.; Davies, D.R.

The mechanism of guanosine triphosphate depletion in the liver after a fructose load. The role of fructokinase

Biochem. J.

228

667-671

1985

Rattus norvegicus

2992452

brenda

641283

Hayward, B.E.; Warner, J.P.; Dunlop, N.; Fantes, J.; Intody, S.; Leek, J.; Markham, A.F.; Bonthron, D.T.

Molecular genetics of the human glucokinase regulator-fructokinase (GCKR-ketohexokinase) region of chromosome 2p23

Biochem. Soc. Trans.

140-145

1997

Homo sapiens

9056860

brenda

Kozak, M.; Hayward, B.; Borek, D.; Bonthron, D.T.; Jaskolski, M.

Expression, purification and preliminary crystallographic studies of human ketohexokinase

Acta Crystallogr. Sect. D

586-588

2001

Homo sapiens

11264590

brenda

Asipu, A.; Hayward, B.E.; O'Reilly, J.; Bonthron, D.T.

Properties of normal and mutant recombinant human ketohexokinases and implications for the pathogenesis of essential fructosuria

Diabetes

2426-2432

2003

Homo sapiens

12941785

brenda

Geigenberger, P.; Regierer, B.; Lytovchenko, A.; Leisse, A.; Schauer, N.; Springer, F.; Kossmann, J.; Fernie, A.R.

Heterologous expression of a ketohexokinase in potato plants leads to inhibited rates of photosynthesis, severe growth retardation and abnormal leaf development

Planta

218

569-578

2004

Rattus norvegicus

14648118

brenda

Giroix, M.H.; Jijakli, H.; Courtois, P.; Zhang, Y.; Sener, A.; Malaisse, W.J.

Fructokinase activity in rat liver, ileum, parotid gland, pancreas, pancreatic islet, B and non-B islet cell homogenates

Int. J. Mol. Med.

517-522

2006

Rattus norvegicus

16465401

brenda

Funari, V.A.; Herrera, V.L.; Freeman, D.; Tolan, D.R.

Genes required for fructose metabolism are expressed in Purkinje cells in the cerebellum

Brain Res. Mol. Brain Res.

142

115-122

2005

Homo sapiens, Mus musculus

16266770

brenda

682791

Hwa, J.S.; Kim, H.J.; Goo, B.M.; Park, H.J.; Kim, C.W.; Chung, K.H.; Park, H.C.; Chang, S.H.; Kim, Y.W.; Kim, D.R.; Cho, G.J.; Choi, W.S.; Kang, K.R.

The expression of ketohexokinase is diminished in human clear cell type of renal cell carcinoma

Proteomics

1077-1084

2006

Homo sapiens (P50053), Homo sapiens

brenda

Trinh, C.H.; Asipu, A.; Bonthron, D.T.; Phillips, S.E.

Structures of alternatively spliced isoforms of human ketohexokinase

Acta Crystallogr. Sect. D

201-211

2009

Homo sapiens (P50053), Homo sapiens

19237742

brenda

706706

Springer, N.; Lindbloom-Hawley, S.; Schermerhorn, T.

Tissue expression of ketohexokinase in cats

Res. Vet. Sci.

115-117

2009

Felis catus

19108855

brenda

Maryanoff, B.; ONeill, J.; McComsey, D.; Yabut, S.; Luci, D.; Jordan Jr., A.; Masucci, J.; Jones, W.; Abad, M.; Gibbs, A.; Petrounia, I.

Inhibitors of ketohexokinase: Discovery of pyrimidinopyrimidines with specific substitution that complements the ATP-binding site

ACS Med. Chem. Lett.

538-543

2011

Homo sapiens

24900346

brenda

723348

Diggle, C.; Shires, M.; McRae, C.; Crellin, D.; Fisher, J.; Carr, I.; Markham, A.; Hayward, B.; Asipu, A.; Bonthron, D.

Both isoforms of ketohexokinase are dispensable for normal growth and development

Physiol. Genomics

42 A

235-243

2010

Mus musculus

20841500

brenda

Rangaswamy, V.; Altekar, W.

Ketohexokinase (ATP:D-fructose 1-phosphotransferase) from a halophilic archaebacterium, Haloarcula vallismortis: purification and properties

J. Bacteriol.

176

5505-5512

1994

Haloarcula vallismortis, Haloarcula vallismortis ATCC 34679

8071229

brenda

737891

Kavitha, R.; Karunagaran, S.; Chandrabose, S.S.; Lee, K.W.; Meganathan, C.

Pharmacophore modeling, virtual screening, molecular docking studies and density functional theory approaches to identify novel ketohexokinase (KHK) inhibitors

BioSystems

138

39-52

2015

Homo sapiens (P50053)

26521124

brenda

737995

Li, X.; Qian, X.; Lu, Z.

Fructokinase A acts as a protein kinase to promote nucleotide synthesis

Cell Cycle

2689-2690

2016

Homo sapiens

27356213

brenda

739133

Li, X.; Qian, X.; Peng, L.X.; Jiang, Y.; Hawke, D.H.; Zheng, Y.; Xia, Y.; Lee, J.H.; Cote, G.; Wang, H.; Wang, L.; Qian, C.N.; Lu, Z.

A splicing switch from ketohexokinase-C to ketohexokinase-A drives hepatocellular carcinomaformation

Nat. Cell Biol.

561-571

2016

Homo sapiens

27088854

brenda

Le, M.; Lanaspa, M.; Cicerchi, C.; Rana, J.; Scholten, J.; Hunter, B.; Rivard, C.; Randolph, R.; Johnson, R.

Bioactivity-guided identification of botanical inhibitors of ketohexokinase

PLoS ONE

e0157458

2016

Homo sapiens

27322374

brenda

Gao, W.; Li, N.; Li, Z.; Xu, J.; Su, C.

Ketohexokinase is involved in fructose utilization and promotes tumor progression in glioma

Biochem. Biophys. Res. Commun.

503

1298-1306

2018

Homo sapiens (P50053), Homo sapiens

30031605

brenda

Steinhauser, C.B.; Landers, M.; Myatt, L.; Burghardt, R.C.; Vallet, J.L.; Bazer, F.W.; Johnson, G.A.

Fructose synthesis and transport at the uterine-placental interface of pigs cell-specific localization of SLC2A5, SLC2A8, and components of the polyol pathway

Biol. Reprod.

108

2016

Sus scrofa

27535960

brenda

Huard, K.; Ahn, K.; Amor, P.; Beebe, D.A.; Borzilleri, K.A.; Chrunyk, B.A.; Coffey, S.B.; Cong, Y.; Conn, E.L.; Culp, J.S.; Dowling, M.S.; Gorgoglione, M.F.; Gutierrez, J.A.; Knafels, J.D.; Lachapelle, E.A.; Pandit, J.; Parris, K.D.; Perez, S.; Pfefferkorn, J.A.; Price, D.A.; Raymer, B.; Ross, T.T.; Shavnya, A.

Discovery of fragment-derived small molecules for in vivo inhibition of ketohexokinase (KHK)

J. Med. Chem.

7835-7849

2017

Homo sapiens (P50053), Homo sapiens, Rattus norvegicus (Q02974)

28853885

brenda

759645

Al-Jawadi, A.; Patel, C.R.; Shiarella, R.J.; Romelus, E.; Auvinen, M.; Guardia, J.; Pearce, S.C.; Kishida, K.; Yu, S.; Gao, N.; Ferraris, R.P.

Cell-type-specific, ketohexokinase-dependent induction by fructose of lipogenic gene expression in mouse small intestine

J. Nutr.

150

1722-1730

2020

Mus musculus (P97328), Mus musculus

32386219

brenda

759646

Hayasaki, T.; Ishimoto, T.; Doke, T.; Hirayama, A.; Soga, T.; Furuhashi, K.; Kato, N.; Kosugi, T.; Tsuboi, N.; Lanaspa, M.A.; Johnson, R.J.; Maruyama, S.; Kadomatsu, K.

Fructose increases the activity of sodium hydrogen exchanger in renal proximal tubules that is dependent on ketohexokinase

J. Nutr. Biochem.

54-62

2019

Mus musculus (P97328)

31276916

brenda