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Information on EC 3.1.3.11 - fructose-bisphosphatase and Organism(s) Homo sapiens and UniProt Accession P09467
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3.1.3.11 fructose-bisphosphataseIUBMB Comments
The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
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Word Map
- 3.1.3.11
- fbpases
-
gluconeogenesis
-
gluconeogenic
- amp
- chloroplast
- phosphoenolpyruvate
-
carboxykinase
- glycogen
- glucose-6-phosphatase
-
phosphofructokinase
- hexokinase
- 2,6-bisphosphate
- spinach
- malate
- thioredoxins
- carboxylase
- starch
- co2
- glucokinase
- phosphorylase
-
6-phosphatase
- fructose-2,6-bisphosphate
- pepck
- trx
- fructose-6-phosphate
- 3-phosphoglycerate
-
nadp-malate
- oleracea
- dihydroxyacetone
- g6pase
- ribulose
- ribulose-1,5-bisphosphate
- triose
-
calvin
- glucagon
- rubisco
-
sucrose-phosphate
-
light-activated
-
amp-dependent
-
antihyperglycemic
- phosphoribulokinase
- 6-phosphofructo-1-kinase
-
calvin-benson
-
monophosphatase
- rubp
- ribulose-5-phosphate
- biofuel production
- synthesis
- medicine
- biotechnology
- molecular biology
- drug development
- diagnostics
-
4.1.1.39
-
t-states
-
2.7.1.11
-
triose-phosphate
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
fructose-1,6-bisphosphatase, fructose 1,6-bisphosphatase, fructose bisphosphatase, fructose-bisphosphatase, fructose 1,6-diphosphatase, fbp-1, fructose diphosphatase, fru-1,6-p2ase, cytosolic fbpase, cfbp1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CY-F1
-
-
-
-
D-fructose 1,6-diphosphatase
-
-
-
-
D-fructose-1,6-bisphosphatase
-
-
-
-
D-fructose-1,6-bisphosphate 1-phosphohydrolase
-
-
-
-
D-fructose-1,6-bisphosphate phosphatase
-
-
-
-
FBPase
Fru-1,6-P2ase
-
-
-
-
fructose 1,6-bisphosphatase
fructose 1,6-bisphosphate 1-phosphatase
-
-
-
-
fructose 1,6-bisphosphate phosphatase
-
-
-
-
fructose 1,6-diphosphatase
-
-
-
-
fructose 1,6-diphosphate phosphatase
-
-
-
-
fructose bisphosphate phosphatase
-
-
-
-
fructose diphosphatase
-
-
-
-
fructose diphosphate phosphatase
-
-
-
-
fructose-1,6-bisphosphatase
hexose bisphosphatase
-
-
-
-
hexose diphosphatase
-
-
-
-
hexosediphosphatase
-
-
-
-
RAE-30
-
-
-
-
FBPase
-
-
-
-
fructose 1,6-bisphosphatase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
D-fructose-1,6-bisphosphate 1-phosphohydrolase
The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
CAS REGISTRY NUMBER
COMMENTARY
9001-52-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
the alkaline isoenzyme may have an important role in vivo in the regulation and control of glycolysis and glyconeogenesis
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
additional information
?
-
-
enzyme together with phosphofructokinase plays a crucial role in metabolism of pancreatic islet cells
-
-
?
additional information
?
-
-
the FBP active site works by stabilizing the FBPase, and the allosteric site impairs the activity of FBPase through its binding of a nonsubstrate molecule. Competitive inhibition of AMP, fructose 1,6-bisphosphate, or fructose 6-phosphate binding to FBPase with fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP)-binding FBPase
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fructose 1,6-diphosphate + H2O
?
-
the alkaline isoenzyme may have an important role in vivo in the regulation and control of glycolysis and glyconeogenesis
-
-
?
additional information
?
-
-
enzyme together with phosphofructokinase plays a crucial role in metabolism of pancreatic islet cells
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
K+
-
at 5 mM Mg2+, increasing K+ up to 140 mM are progressively inhibitory for neutral and alkaline isoenzyme from liver, muscle neutral isoenzyme is activated, 10% at 5 mM Mg2+ but inhibited at 1 mM Mg2+
Mg2+
Mn2+
Mg2+
wild-type muscle enzyme, Hill coefficient 1.89, wild-type liver enzyme, hill coefficient 1.83
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl)methyl dihydrogen phosphate
-
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)methyl dihydrogen phosphate
-
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl)methyl dihydrogen phosphate
-
(2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl)methyl dihydrogen phosphate
-
(2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl)phosphonic acid
-
(4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol
i.e. PFE, allosteric inhibitor
1-(cyclopropyl)methyl-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
-
2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate
wild-type muscle enzyme, 50% inhibition at 0.00022 mM, wild-type liver enzyme, 50% inhibition at 0.0046 mM
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl dihydrogen phosphate
-
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl dihydrogen phosphate
-
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl dihydrogen phosphate
-
2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl dihydrogen phosphate
-
3-(2-carboxyethyl)-4-(2-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(3-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(3-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(4-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(4-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-(3-methoxyphenylamino)-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-(3-nitrophenyl)-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-(4-methoxyphenylamino)-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-(4-nitrophenyl)-1H-indole-2-carboxylic acid
-
ethyl 2-[((5-[2-amino-5-(2,2-dimethylpropanoyl)-1,3-thiazol-4-yl]furan-2-yl)[(1-ethoxy-2-methyl-1-oxopropan-2-yl)amino]phosphoryl)amino]-2-methylpropanoate
MB07803
fructose 2,6-diphosphate
lung enzyme is slightly more sensitive to inhibition than the liver enzyme. Synergistic effect of AMP and fructose 2,6-diphosphate on lung and liver enzyme
[(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)(difluoro)methyl]phosphonic acid
-
[(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)methyl]phosphonic acid
-
[2-[[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]amino]ethyl]phosphonate
-
[3-[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]propyl]phosphonate
-
[5-(4-amino-1-tert-butyl-2,3-dihydro-1H-benzimidazol-2-yl)-2-furyl]phosphonate
-
[5-(4-amino-1-tert-butyl-7-ethyl-5-fluoro-2,3-dihydro-1H-benzimidazol-2-yl)-2-furyl]phosphonate
-
[5-(6-amino-9-tert-butyl-8,9-dihydro-7H-purin-8-yl)-2-furyl]phosphonate
-
[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
-
[5-[6-amino-9-(2,2-dimethylpropyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
-
[5-[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
-
[5-[6-amino-9-(2-phenylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
-
-
(3-Bromo-phenyl)-(6,7-dimethoxy-2-methyl-quinazolin-4-yl)-amine
-
IC50: 0.0045 mM
(3-Bromo-phenyl)-[7-methoxy-6-(2-methoxy-ethoxy)-quinazolin-4-yl]-amine
-
IC50: 0.0055 mM
(3-Chloro-4-fluoro-phenyl)-(6,7-diethoxy-quinazolin-4-yl)-amine
-
IC50: 0.00053 mM
(5-[2-amino-5-[(propylsulfanyl)carbonyl]-1,3-thiazol-4-yl]furan-2-yl)phosphonic acid
-
-
(5-[4-amino-7-[3-(dimethylamino)propyl]-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl)phosphonic acid
-
-
2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate
-
able to bind not only to the AMP allosteric site but also to the fructose-1,6-bisphosphate active site
2,5-dichloro-N-[5-methoxy-7-(4-methoxypyridin-3-yl)-1,3-benzoxazol-2-yl]benzenesulfonamide
-
-
2,5-dichloro-N-[7-(3-hydroxyphenyl)-5-methoxy-1,3-benzoxazol-2-yl]benzenesulfonamide
-
-
2,5-dichloro-N-[7-(4-hydroxyphenyl)-5-methoxy-1,3-benzoxazol-2-yl]benzenesulfonamide
-
-
2-(2-aminoethyl)-6,7-diethoxy-N-[3-(2-methyl-1,3-thiazol-4-yl)phenyl]quinazolin-4-amine
-
uncompetitive
2-amino-4-[2-(5-(1-(3-bromophenyl)-1,3-propyl)phosphono)-furanyl]-5-isobutyl-thiazole
-
-
2-amino-4-[2-(5-(O-phenyl)-(N-((S)-1-ethoxycarbonyl)ethyl)-phosphonamido)-furanyl]-5-isobutylthiazole
-
-
2-amino-4-[2-(5-N,N'-bis((S)-1-(1-ethoxycarbonyl)ethyl)phosphonoamido)furanyl]-5-isobutylthiazole
-
optimization of the diamide prodrugs of phosphonic acid leads to the identification of a new diamide, the first reported orally efficacious FBPase inhibitor
2-amino-4-[2-(5-phosphono)furanyl]-5-ethoxycarbonylthiazole
-
potent FBPase inhibitor
2-amino-4-[2-(5-phosphono)furanyl]-5-propylsulfanylthiazole
-
potent FBPase inhibitor
2-amino-4-[2-[5-(1-(4-pyridyl)-1,3-propyl)phosphono]furanyl]-5-isobutylthiazole
-
-
2-amino-4-[2-[5-bis(1-(1-ethoxycarbonyloxy)ethyl)phosphono]-furanyl]-5-isobutyl-thiazole
-
-
2-amino-4-[2-[5-bis(ethoxycarbonyloxymethyl)phosphono]-furanyl]-5-isobutyl-thiazole
-
-
2-amino-4-[2-[5-bis(phenoxycarbonyloxymethyl)phosphono]-furanyl]-5-isobutyl-thiazole
-
-
2-amino-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
poor oral bioavailability
2-amino-5-methylsulfanyl-4-[2-(5-diethylphosphono)furanyl]thiazole
-
potent FBPase inhibitor
2-amino-5-[(4-morpholinyl)methyl]-4-[2-(5-phosphono)furanyl]-thiazole dihydrobromide
-
-
2-[(3S,11aS)-3-(4-hydroxybenzyl)-1,4-dioxo-1,3,4,6,11,11a-hexahydro-2H-pyrazino[1,2-b]isoquinolin-2-yl]-N-[2-(4-hydroxyphenyl)ethyl]pentanamide
-
uncompetitive
2-[3-methyl-5-([[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)thiophen-2-yl]ethyl acetate
-
-
2-[5-([[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)-3-methylthiophen-2-yl]ethyl acetate
-
-
3-(2-carboxyethyl)-4-(2-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(2-methylpropyl)-7-nitro-1H-indole-2-carboxylic acid
-
-
3-(2-carboxyethyl)-4-(3-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(3-methoxyanilino)-7-nitro-1H-indole-2-carboxylic acid
-
-
3-(2-carboxyethyl)-4-(3-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(4-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(4-methoxyanilino)-7-nitro-1H-indole-2-carboxylic acid
-
-
3-(2-carboxyethyl)-4-(4-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-5-(2-methylpropyl)-7-nitro-1H-indole-2-carboxylic acid
-
-
3-(2-carboxyethyl)-7-nitro-4-(3-methoxyphenylamino)-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-(3-nitrophenyl)-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-(4-methoxyphenylamino)-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-(4-nitrophenyl)-1H-indole-2-carboxylic acid
-
3-ethyl-5-isobutyl-7-nitro-1H-indole-2-carboxylic acid
-
molecular modeling of binding mode. The key hydrogen bonding interactions are observed between the carboxylate and residues Thr 27, Lys 112 and Arg 140, which are also recognized by the phosphate group in AMP. This hydrogen bonding network may make crucial contributions to the binding affinity. The indole ring is situated in a hydrophobic pocket involved in residues Leu30 and Leu34. The 7-nitro group interacted with the hydroxyl group of Thr31 via a hydrogen bond
4-anilinoquinazoline
-
low molecular weight inhibitors of enzyme that are not substrate mimics or AMP analogues
5-(1H-tetrazol-5-yl)-N-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenyl)pentanamide
-
-
5-(2-hydroxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-4-methyl-N-([6-[(methylcarbamoyl)amino]-4-(methylsulfanyl)pyridin-2-yl]carbamoyl)thiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-4-methyl-N-[[4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-N-([4-methoxy-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-4-methylthiophene-2-sulfonamide
-
-
diethyl (5-[4-amino-1-[(1R,2R)-bicyclo[2.2.1]hept-2-ylamino]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl (5-[4-amino-1-[3-(thiophen-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl (5-[4-amino-1-[4-(furan-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl (5-[4-amino-1-[4-(trifluoromethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl [5-[4-amino-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(3-hydroxybenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(4-tert-butylbenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(biphenyl-4-ylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclobutylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cycloheptylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclohexylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclopentylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclopropylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diphenyl [5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonate
-
non-competitive
ethyl (2S,6S)-4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-2,6-dimethyl-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide
-
-
ethyl 4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-2,2,6,6-tetramethyl-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide (non-preferred name)
-
-
ethyl 4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-2,6-dimethyl-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide (non-preferred name)
-
-
ethyl 4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide (non-preferred name)
-
-
K+
-
at 5 mM Mg2+, increasing K+ up to 140 mM are progressively inhibitory for neutral and alkaline isoenzyme from liver, muscle neutral isoenzyme is activated, 10% at 5 mM Mg2+ but inhibited at 1 mM Mg2+
N,N'-bis(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)pentane-1,5-diamine
-
uncompetitive
N-([4-bromo-6-[(2,2,2-trifluoroethyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-([4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(6-amino-4-bromopyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(6-amino-4-methoxypyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(7-bromoimidazo[1,2-a]pyridin-5-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[6-(4-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
-
non-competitive
N-[7-(3-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
-
-
N-[7-(4-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
-
-
N-[7-[3-(aminomethyl)phenyl]-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
-
-
N-[[6-amino-4-(methylsulfanyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[[6-amino-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-hydroxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
NH4+
-
0.01-0.02 mM, slight activation of neutral and alkaline isoenzyme, progressive inhibition at increasing concentration
propan-2-yl 4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-9-methyl-7-oxo-3,5,8-trioxa-4-phosphadecan-1-oate 4-oxide
-
-
tert-butyl 4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-9,9-dimethyl-7-oxo-3,5,8-trioxa-4-phosphadecan-1-oate 4-oxide
-
-
TNP-AMP
-
a fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP), is used as a fluorescent probe as it is able to competitively inhibit AMP binding to the AMP allosteric site. AMP and fructose 1,6-bisphosphate both can reduce the fluorescence from the bound TNP-AMP through competition for FBPase, suggesting that TNP-AMP binds not only to the AMP allosteric site but also to the FBP active site. The residue K274 is very important for TNP-AMP to bind to the active site of FBPase. When the residue K274 is mutated to L274, TNP-AMP cannot bind to the active site, but can bind to the allosteric site
Zn2+
-
0.001-0.010 mM has no significant effect, with 0.002-0.0035 mM Zn2+, in absence of EDTA, 50% inhibition, 80% inhibition by 0.01 mM Zn2+
[(2R,3S,4R,5R)-5-[4-(aminocarbonyl)-1H-imidazol-1-yl]-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen phosphate
-
-
[5-(2-amino-5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
non-competitive
[5-(4-amino-5-bromo-1-cyclopropyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonic acid
-
-
[5-[2-amino-5-(2-methylpropyl)-1,3-selenazol-4-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-1-(2-ethylbutyl)-5-fluoro-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5,7-dibromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-bromo-6,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-ethyl-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-phenyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-propyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(pentan-3-yl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-7-(2-methoxyethyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-7-(3-methylbutyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-7-(4-fluorophenyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-hydroxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-6-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-(3,3-dimethylbutyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-(4-chlorophenyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-(6-chlorohexyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-bromo-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-cyclopropyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-ethenyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-ethyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
AMP
wild-type muscle enzyme, 50% inhibition at 0.0001 mM, Hill coefficient 1.78, wild-type liver enzyme, 50% inhibition at 0.0044 mM, Hill coefficient 2.08
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
non-competitive
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
50% inhibition at 0.0034 mM
AMP
-
113Tyr and 31Thr play an mportant role, each via two hydrogen bonds affecting the binding affinity of inhibitor AMP to FBPase
AMP
-
allosteric inhibition. The fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP), is used as a fluorescent probe as it is able to competitively inhibit AMP binding to the AMP allosteric site
AMP
inactive, AMP-associated T state of the enzyme, AMP binding results in improved thermal stability of muscle FBPase
Ca2+
-
Ca2+ affects conformation of the catalytic loop 52-72 of muscle FBPase and inhibits its activity by competing with activatory divalent cations, e.g. Mg2+ and Zn2+. Aldolase associates with FBPase in its active form, i.e. with loop 52-72 in the engaged conformation, while Ca2+ stabilizes the disengaged-like form of the loop
additional information
-
a series of novel indole derivatives is designed and synthesized as inhibitors of fructose-1,6-bisphosphatase (FBPase), structure-activity relationships, molecular docking, overview. No inhibition by 3-(2-carboxyethyl)-4-nitro-1H-indole-2-carboxylic acid and 3-(2-carboxyethyl)-6-nitro-1H-indole-2-carboxylic acid
-
additional information
a series of novel indole derivatives is designed and synthesized as inhibitors of fructose-1,6-bisphosphatase (FBPase), structure-activity relationships, molecular docking, overview. No inhibition by 3-(2-carboxyethyl)-4-nitro-1H-indole-2-carboxylic acid and 3-(2-carboxyethyl)-6-nitro-1H-indole-2-carboxylic acid
-
additional information
the FBPase pig kidney tetramer overlay of human and pig kidney (PDB IDs 1FTA and 1KZ8, respectively) show nearly identical orientation and conformation in the active site, AMP allosteric binding site, and inhibitor (4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol allosteric binding site architecture
-
additional information
-
the FBPase pig kidney tetramer overlay of human and pig kidney (PDB IDs 1FTA and 1KZ8, respectively) show nearly identical orientation and conformation in the active site, AMP allosteric binding site, and inhibitor (4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol allosteric binding site architecture
-
additional information
-
design, synthesis, and structure-activity relationship of a series of phosphonic acid containing benzimidazoles that function as fructose-1,6-bisphosphatase inhibitors and AMP mimics
-
additional information
-
inhibitor design, synthesis and molecular modeling, overview
-
additional information
-
synthesis and evaluation of a series of phosphonic acid-containing thiazoles as enzyme inhibitors, structure-guided drug design approach, optimization of both the thiazole FBPase inhibitors and their prodrugs, overview
-
additional information
mammalian muscle FBPase is about 100times more susceptible to the allosteric inhibitors AMP and NAD+ and about 1000times more sensitive to inhibition by Ca2+ than the liver isozyme
-
additional information
-
mammalian muscle FBPase is about 100times more susceptible to the allosteric inhibitors AMP and NAD+ and about 1000times more sensitive to inhibition by Ca2+ than the liver isozyme
-
additional information
-
the FBP active site works by stabilizing the FBPase, and the allosteric site impairs the activity of FBPase through its binding of a nonsubstrate molecule. Competitive inhibition of AMP, fructose 1,6-bisphosphate, or fructose 6-phosphate binding to FBPase with fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP)-binding FBPase
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AMP
-
20% activation at 0.001-0.002 mM of AMP at alkaline pH, KM value of 0.00018 mM at pH 7.5, 30°C, recombinant enzyme
NH4+
-
0.01-0.02 mM, slight activation of neutral and alkaline isoenzyme, progressive inhibition at increasing concentration
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0015
D-fructose 1,6-bisphosphate
liver enzyme mutant E20K/M177T/C179Q, pH 7.5, 37°C
0.0015
D-fructose 1,6-bisphosphate
muscle enzyme mutant T177M/Q179C, pH 7.5, 37°C
0.0017
D-fructose 1,6-bisphosphate
muscle enzyme mutant K20E/T177M/Q179C, pH 7.5, 37°C
0.0019
D-fructose 1,6-bisphosphate
liver enzyme mutant M177T/C179Q, pH 7.5, 37°C
0.0019
D-fructose 1,6-bisphosphate
muscle enzyme mutant K20E, pH 7.5, 37°C
0.0023
D-fructose 1,6-bisphosphate
liver enzyme mutant E20K, pH 7.5, 37°C
0.018
D-fructose 1,6-bisphosphate
-
pH 7.4, temperature not specified in the publication, wild-type enzyme
0.04
D-fructose 1,6-bisphosphate
-
pH 7.4, temperature not specified in the publication, mutant enzyme K274L
additional information
additional information
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.6
D-fructose 1,6-bisphosphate
muscle enzyme mutant K20E/T177M/Q179C, pH 7.5, 37°C
18.4
D-fructose 1,6-bisphosphate
liver enzyme mutant M177T/C179Q, pH 7.5, 37°C
19.9
D-fructose 1,6-bisphosphate
muscle enzyme mutant T177M/Q179C, pH 7.5, 37°C
21.7
D-fructose 1,6-bisphosphate
liver enzyme mutant E20K/M177T/C179Q, pH 7.5, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00013
D-fructose 1,6-bisphosphate
muscle enzyme mutant T177M/Q179C, pH 7.5, 37°C
0.00016
D-fructose 1,6-bisphosphate
muscle enzyme mutant K20E/T177M/Q179C, pH 7.5, 37°C
0.00016
D-fructose 1,6-bisphosphate
wild-type muscle enzyme, pH 7.5, 37°C
0.00017
D-fructose 1,6-bisphosphate
muscle enzyme mutant K20E, pH 7.5, 37°C
0.00018
D-fructose 1,6-bisphosphate
liver enzyme mutant E20K/M177T/C179Q, pH 7.5, 37°C
0.00019
D-fructose 1,6-bisphosphate
liver enzyme mutant M177T/C179Q, pH 7.5, 37°C
0.00024
D-fructose 1,6-bisphosphate
liver enzyme mutant E20K, pH 7.5, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0164
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.354
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl)phosphonic acid
Homo sapiens
-
0.0191
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.00932
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)phosphonic acid
Homo sapiens
-
0.0215
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.354
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl)phosphonic acid
Homo sapiens
-
0.0417
(2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.000169
(2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl)phosphonic acid
Homo sapiens
-
0.000124
(2-amino-8H-indeno[1,2-d][1,3]thiazol-4-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.112
(2-amino-8H-indeno[1,2-d][1,3]thiazol-5-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.112
(2-amino-8H-indeno[1,2-d][1,3]thiazol-6-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.05
1-(cyclopropyl)methyl-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
above, pH 7.5, 37°C, recombinant His-tagged enzyme
0.05
1-benzyl-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
above, pH 7.5, 37°C, recombinant His-tagged enzyme
0.112
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl dihydrogen phosphate
Homo sapiens
-
0.000013
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl dihydrogen phosphate
Homo sapiens
-
0.335
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl dihydrogen phosphate
Homo sapiens
-
0.000022
2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl dihydrogen phosphate
Homo sapiens
-
0.05
3-(2-(ethoxycarbonyl)-7-nitro-1H-indol-3-yl)propanoic acid
Homo sapiens
above, pH 7.5, 37°C, recombinant His-tagged enzyme
0.0024
3-(2-carboxyethyl)-4-(2-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00527
3-(2-carboxyethyl)-4-(3-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00522
3-(2-carboxyethyl)-4-(3-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0024
3-(2-carboxyethyl)-4-(4-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0018
3-(2-carboxyethyl)-4-(4-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00088
3-(2-carboxyethyl)-4-chloro-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00276
3-(2-carboxyethyl)-4-ethyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00069
3-(2-carboxyethyl)-4-isobutyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00129
3-(2-carboxyethyl)-5-bromo-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00207
3-(2-carboxyethyl)-5-chloro-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0001
3-(2-carboxyethyl)-5-ethyl-7-nitro-1H-indole-2-carboxylicacid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00045
3-(2-carboxyethyl)-5-isobutyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.05
3-(2-carboxyethyl)-5-nitro-1H-indole-2-carboxylic acid
Homo sapiens
above, pH 7.5, 37°C, recombinant His-tagged enzyme
0.0016
3-(2-carboxyethyl)-5-phenylamino-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00517
3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00131
3-(2-carboxyethyl)-7-nitro-4-(3-methoxyphenylamino)-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0011
3-(2-carboxyethyl)-7-nitro-4-(3-nitrophenyl)-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0017
3-(2-carboxyethyl)-7-nitro-4-(4-methoxyphenylamino)-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.002
3-(2-carboxyethyl)-7-nitro-4-(4-nitrophenyl)-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0014
3-(2-carboxyethyl)-7-nitro-4-phenyl-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00069
3-(2-carboxyethyl)-7-nitro-4-phenylamino-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00643
3-(2-carboxyethyl)-7-nitro-5-phenyl-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.05
7-amino-3-(2-carboxyethyl)-1H-indole-2-carboxylic acid
Homo sapiens
above, pH 7.5, 37°C, recombinant His-tagged enzyme
0.000047
[(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)(difluoro)methyl]phosphonic acid
Homo sapiens
-
0.00084
[(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)methyl]phosphonic acid
Homo sapiens
-
0.097
[2-[[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]amino]ethyl]phosphonate
Homo sapiens
-
0.026
[3-[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]propyl]phosphonate
Homo sapiens
-
0.0016
[5-(4-amino-1-tert-butyl-2,3-dihydro-1H-benzimidazol-2-yl)-2-furyl]phosphonate
Homo sapiens
-
0.00009
[5-(4-amino-1-tert-butyl-7-ethyl-5-fluoro-2,3-dihydro-1H-benzimidazol-2-yl)-2-furyl]phosphonate
Homo sapiens
-
0.0022
[5-(6-amino-9-tert-butyl-8,9-dihydro-7H-purin-8-yl)-2-furyl]phosphonate
Homo sapiens
-
0.000001
[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
0.0011
[5-[6-amino-9-(2,2-dimethylpropyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
Homo sapiens
-
0.0012
[5-[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
Homo sapiens
-
0.005 - 0.015
[5-[6-amino-9-(2-phenylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
0.00029
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0045
(3-Bromo-phenyl)-(6,7-dimethoxy-2-methyl-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.0045 mM
0.0039
(3-Bromo-phenyl)-(7-ethoxy-6-nitro-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.0039 mM
0.0029
(3-Bromo-phenyl)-[6-(2-methoxy-ethoxy)-quinazolin-4-yl]-amine
Homo sapiens
-
IC50: 0.0029 mM
0.0055
(3-Bromo-phenyl)-[7-methoxy-6-(2-methoxy-ethoxy)-quinazolin-4-yl]-amine
Homo sapiens
-
IC50: 0.0055 mM
0.00053
(3-Chloro-4-fluoro-phenyl)-(6,7-diethoxy-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.00053 mM
0.0013
(3-Chloro-phenyl)-(6,7-dimethoxy-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.0013 mM
0.000858
(5-[2-amino-5-[(propylsulfanyl)carbonyl]-1,3-thiazol-4-yl]furan-2-yl)phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000055
(5-[4-amino-7-[3-(dimethylamino)propyl]-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl)phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0024
(6,7-Diethoxy-quinazolin-4-yl)-(3-ethynyl-phenyl)-amine
Homo sapiens
-
IC50: 0.0024 mM
0.0009
(6,7-Dimethoxy-quinazolin-4-yl)-(3-ethynyl-phenyl)-amine
Homo sapiens
-
IC50: 0.0009 mM
0.0035
2,5-dichloro-N-[5-methoxy-7-(4-methoxypyridin-3-yl)-1,3-benzoxazol-2-yl]benzenesulfonamide
Homo sapiens
-
-
0.0017
2,5-dichloro-N-[7-(3-hydroxyphenyl)-5-methoxy-1,3-benzoxazol-2-yl]benzenesulfonamide
Homo sapiens
-
-
0.0018
2,5-dichloro-N-[7-(4-hydroxyphenyl)-5-methoxy-1,3-benzoxazol-2-yl]benzenesulfonamide
Homo sapiens
-
-
0.00022
2-(2-aminoethyl)-6,7-diethoxy-N-[3-(2-methyl-1,3-thiazol-4-yl)phenyl]quinazolin-4-amine
Homo sapiens
-
uncompetitive
0.008
2-(2-thienyl)-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.005
2-(3-pyridyl)-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.01
2-acetamido-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0013
2-amino-4-[1-(3-phosphono)phenyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
2-amino-4-[2-(6-phosphono)pyridyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000028
2-amino-5-(2,2,2-trifluoroethyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00004
2-amino-5-(2-furanyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000043
2-amino-5-(2-methoxyphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000012
2-amino-5-(2-naphthyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.95
2-amino-5-(2-thienyl)-4-[(N-phosphonomethyl)carbamoyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000044
2-amino-5-(2-thienyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000021
2-amino-5-(3-methoxyphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000032
2-amino-5-(4-acetylphenyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000013
2-amino-5-(4-chlorophenyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000016
2-amino-5-(4-fluorophenyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000041
2-amino-5-(4-methanesulfonyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000014
2-amino-5-(4-methoxycarbonylphenyl)-4-[2-(5-phosphono)-furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000022
2-amino-5-(4-methoxyphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000021
2-amino-5-(4-methylthiophenyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000034
2-amino-5-(4-phenylphenyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000088
2-amino-5-(4-tert-butylphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000016
2-amino-5-(N-morpholinyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000059
2-amino-5-benzyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000015
2-amino-5-benzyloxycarbonyl-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00005
2-amino-5-bromo-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00007
2-amino-5-chloro-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000012
2-amino-5-cyclobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000021
2-amino-5-cyclohexyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000018
2-amino-5-cyclohexylmethyl-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000019
2-amino-5-cyclopentyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00002
2-amino-5-cyclopentylmethyl-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00001
2-amino-5-cyclopropylmethyl-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000033
2-amino-5-ethylthio-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00012
2-amino-5-hydroxymethyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
2-amino-5-iodo-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.21
2-amino-5-isopropyl- 4-[1-(4-methoxy-3-phosphono)phenyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00003
2-amino-5-isopropyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000024
2-amino-5-isopropylthio-4-[2-(5-phosphono)furanyl]thiazole hydrobromide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00045
2-amino-5-methyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000057
2-amino-5-neopentyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.08
2-amino-5-phenyl- 4-[1-(4-fluoro-3-phosphono)phenyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.01
2-amino-5-phenyl-4-[2-(5-methyl-4-phosphono)oxazolyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.01
2-amino-5-phenyl-4-[3-(1-phosphono)pyrrolyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0003
2-amino-5-phenylthio-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.135
2-amino-5-propyl- 4-[1-(4-methyl-3-phosphono)phenyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.05
2-amino-5-propyl-4-phosphonomethoxycarbonylthiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.25
2-amino-5-propyl-4-[1-(3-phosphono)phenyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0005
2-amino-5-propyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000024
2-amino-5-tert-butylthio-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00015
2-amino-5-[(4-morpholinyl)methyl]-4-[2-(5-phosphono)furanyl]-thiazole dihydrobromide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0017
2-amino-5-[(N,N-dimethyl)carbamoyl]-4-[2-(5-phosphono)-furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00008
2-bromo-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00275
2-carbamoyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00018
2-chloro-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
2-cyano-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0004
2-ethyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00022
2-hydroxymethyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
2-methyl-5-isobutyl-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.001
2-methylamino-5-isobutyl-4-[2-(5-hosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00089
2-methylthio-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0135
2-phenyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0005
2-thiocarbamoyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0012
2-vinyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00187
2-[(3S,11aS)-3-(4-hydroxybenzyl)-1,4-dioxo-1,3,4,6,11,11a-hexahydro-2H-pyrazino[1,2-b]isoquinolin-2-yl]-N-[2-(4-hydroxyphenyl)ethyl]pentanamide
Homo sapiens
-
uncompetitive
0.00052
2-[3-methyl-5-([[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)thiophen-2-yl]ethyl acetate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00067
2-[5-([[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)-3-methylthiophen-2-yl]ethyl acetate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0025
3-(2-carboxyethyl)-4,6-dichloro-1H-indole-2-carboxylic acid
Homo sapiens
-
non-competitive
0.0024
3-(2-carboxyethyl)-4-(2-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00069
3-(2-carboxyethyl)-4-(2-methylpropyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
-
0.00527
3-(2-carboxyethyl)-4-(3-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00131
3-(2-carboxyethyl)-4-(3-methoxyanilino)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
-
0.00522
3-(2-carboxyethyl)-4-(3-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0024
3-(2-carboxyethyl)-4-(4-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0017
3-(2-carboxyethyl)-4-(4-methoxyanilino)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
-
0.0018
3-(2-carboxyethyl)-4-(4-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00088
3-(2-carboxyethyl)-4-chloro-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00276
3-(2-carboxyethyl)-4-ethyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00045
3-(2-carboxyethyl)-5-(2-methylpropyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
-
0.00207
3-(2-carboxyethyl)-5-chloro-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0001
3-(2-carboxyethyl)-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00517
3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0011
3-(2-carboxyethyl)-7-nitro-4-(3-nitrophenyl)-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.002
3-(2-carboxyethyl)-7-nitro-4-(4-nitrophenyl)-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0014
3-(2-carboxyethyl)-7-nitro-4-phenyl-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00643
3-(2-carboxyethyl)-7-nitro-5-phenyl-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00064
3-chloro-N-[(3,5-dichlorophenyl)carbamoyl]benzenesulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00069
4-anilino-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
-
0.00298
5-(1H-tetrazol-5-yl)-N-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenyl)pentanamide
Homo sapiens
-
pH 7.5, temperature not specified in the publication
0.00035
5-(2-hydroxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00017
5-(2-methoxyethyl)-4-methyl-N-([6-[(methylcarbamoyl)amino]-4-(methylsulfanyl)pyridin-2-yl]carbamoyl)thiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0017
5-(2-methoxyethyl)-4-methyl-N-[[4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00053
5-(2-methoxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00022
5-(2-methoxyethyl)-N-([4-methoxy-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0016
5-anilino-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
-
0.00129
5-bromo-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
-
0.0005
5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00132
6-hydroxy-N-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenyl)hexanamide
Homo sapiens
-
pH 7.5, temperature not specified in the publication
0.00532
6-oxo-6-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenylamino)hexanoic acid
Homo sapiens
-
pH 7.5, temperature not specified in the publication
0.002
diethyl (5-[4-amino-1-[(1R,2R)-bicyclo[2.2.1]hept-2-ylamino]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.004
diethyl (5-[4-amino-1-[3-(thiophen-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0042
diethyl (5-[4-amino-1-[4-(furan-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.007
diethyl (5-[4-amino-1-[4-(trifluoromethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.005
diethyl [5-(4-amino-1-benzyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00225
diethyl [5-(4-amino-1-ethyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.006
diethyl [5-(4-amino-1-methyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0011
diethyl [5-(4-amino-1-propyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0015
diethyl [5-[4-amino-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00185
diethyl [5-[4-amino-1-(3-hydroxybenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0095
diethyl [5-[4-amino-1-(4-tert-butylbenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0025
diethyl [5-[4-amino-1-(biphenyl-4-ylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0008
diethyl [5-[4-amino-1-(cyclobutylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00325
diethyl [5-[4-amino-1-(cycloheptylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0025
diethyl [5-[4-amino-1-(cyclohexylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0015
diethyl [5-[4-amino-1-(cyclopentylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0008
diethyl [5-[4-amino-1-(cyclopropylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0026
N,N'-bis(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)pentane-1,5-diamine
Homo sapiens
-
uncompetitive
0.023
N-(5-chloro-1,3-benzoxazol-2-yl)-2-(1H-imidazol-1-yl)benzenesulfonamide
Homo sapiens
-
-
0.0078
N-(5-chloro-1,3-benzoxazol-2-yl)-4-(trifluoromethoxy)benzenesulfonamide
Homo sapiens
-
-
0.0002
N-([4-bromo-6-[(2,2,2-trifluoroethyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00008
N-([4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00033
N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3-chlorobenzenesulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00013
N-[(6-amino-4-bromopyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0004
N-[(6-amino-4-methoxypyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00033
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00014
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00035
N-[(6-bromo-1H-indol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00082
N-[(7-bromoimidazo[1,2-a]pyridin-5-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00057
N-[6-(4-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
non-competitive
0.00057
N-[7-(3-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
-
0.0013
N-[7-(4-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
-
0.0026
N-[7-[3-(aminomethyl)phenyl]-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
-
0.0018
N-[[6-amino-4-(methylsulfanyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00076
N-[[6-amino-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00042
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-hydroxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0006
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.012
[(2R,3S,4R,5R)-5-[4-(aminocarbonyl)-1H-imidazol-1-yl]-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen phosphate
Homo sapiens
-
-
0.000016
[5-(2-amino-5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Homo sapiens
-
non-competitive
0.000014
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.01
[5-(2-amino-5-propyl-1,3-thiazol-4-yl)thiophen-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000055
[5-(4-amino-5-bromo-1-cyclopropyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000039
[5-[2-amino-5-(2-methylpropyl)-1,3-selenazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
-
0.000025
[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000014
[5-[2-amino-5-(ethoxycarbonyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000016
[5-[2-amino-5-(propylsulfanyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00015
[5-[4-amino-1-(2-ethylbutyl)-5-fluoro-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.001
[5-[4-amino-5,7-dibromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00045
[5-[4-amino-5,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0004
[5-[4-amino-5-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.01
[5-[4-amino-5-bromo-6,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0002
[5-[4-amino-5-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0025
[5-[4-amino-5-ethyl-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00009
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-phenyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-propyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00085
[5-[4-amino-5-fluoro-1-(pentan-3-yl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00008
[5-[4-amino-5-fluoro-7-(2-methoxyethyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
[5-[4-amino-5-fluoro-7-(3-methylbutyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00018
[5-[4-amino-5-fluoro-7-(4-fluorophenyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0005
[5-[4-amino-5-hydroxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0007 - 0.003
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.000225
[5-[4-amino-6-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00021
[5-[4-amino-7-(3,3-dimethylbutyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00009
[5-[4-amino-7-(4-chlorophenyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00007
[5-[4-amino-7-(6-chlorohexyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0004
[5-[4-amino-7-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00013
[5-[4-amino-7-bromo-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0009
[5-[4-amino-7-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
[5-[4-amino-7-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00006
[5-[4-amino-7-cyclopropyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00028
[5-[4-amino-7-ethenyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000055
[5-[4-amino-7-ethyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00056
[5-[5-(2-methylpropyl)-2-phenyl-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.005
[5-[6-amino-9-(2-phenylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
Homo sapiens
-
0.015
[5-[6-amino-9-(2-phenylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
Homo sapiens
-
0.0034
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
non-competitive
0.0025
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfonamide
Homo sapiens
-
non-competitive
0.0007
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.003
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5
8
-
mutant carrying insertion of cysteine-rich light regulatory sequence of Pisum sativum enzyme into corresponding site of Beta vulgaris enzyme
8.5
-
chimeric enzyme of C-terminal half of Beta vulgaris with C-terminal half of Pisum sativum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
FBP1 is commonly upregulated in tumor tissues compared with non-tumor tissues regardless of histological type. Enzyme expression profiles of breast cancer cells reveals that cells exhibiting high expression of FBP1 have a lower activity of Wnt/beta-catenin pathway
FBP1 is commonly upregulated in tumor tissues compared with non-tumor tissues regardless of histological type
-
the amount of polymorphonuclear and mononuclear cells with positive FBPase immunocytochemical reaction is 57% and 68%, respectively in patients with type 1 diabetes mellitus, and 38% and 42%, respectively in healthy donors
additional information
-
-
170787, 170788, 170790, 170806, 650448, 650877, 679512, 682776, 690771, 714432, 715844, 715855, 729390, 750474
-
peripheral blood monocyte. baseline activity of fructose 1,6-bisphosphatase in cancer patients is 1.0 nmol/min/mg protein, and 4.4 nmol/min/mg for healthy volunteers
-
the muscle enzyme is located on both sides of the Z line, in the isotropic regions of myocytes, the muscle enzyme binds strongly to alpha-actinin, a major structural protein of the Z line
additional information
-
in tumor cell lines, demethylation with 5-aza-deoxycytidine activates the expression of both L- and M-fructose 1,6-bisphosphatase. Additional inhibition of histone deacetylase with trichostatin A further increases FBPase mRNA concentrations
additional information
-
when non-malignant and malignant tissue samples from the same patient are compared a correlation between an increase of FBPase promoter methylation and a decrease of FBPase mRNA levels is observed
additional information
the muscle FBPase FBP2 is also present in cells that predominantly express the liver isozyme FBP1, e.g. in the liver itself
additional information
-
the muscle FBPase FBP2 is also present in cells that predominantly express the liver isozyme FBP1, e.g. in the liver itself
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
integrity of the 203KKKGK207 motif is crucial to nuclear targeting. Even a single amino-acid change within this sequence results in significant decrease of nuclear accumulation of the enzyme
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
enzyme FBPase is a key rate-controlling enzyme in the gluconeogenic pathway
physiological function
metabolism
physiological function
additional information
malfunction
genetic silencing of enzyme fructose-1,6-bisphosphatase (FBP1) reduces aerobic glycolysis and the malignant potential of breast cancer cells. FBP1 down-regulation enhances the activity of Wnt/b-Catenin pathway and increases the level of its downstream targets, including c-Myc and MMP7
malfunction
two significant mutations in the coding region of the FBPase gene in patients with hypoglycemia link the AMP-binding site to the active site of the enzyme. Individuals with FBPase deficiency exhibit hypoglycemia and metabolic acidosis due to impaired gluconeogenesis. In rare cases, hypoglycemia, an autosomal recessive disorder characterized by insufficient blood glucose levels, is genetically linked to FBPase deficiency in clinical studies. The M177 and Y164 interfacial residues are positioned between the AMP-binding site and active sites and are mutated in humans with hypoglycemia
physiological function
compared with negative littermates, liver-specific FBPase transgenic mice have 50% less adiposity and eat 15% less food but do not have altered energy expenditure. The reduced food consumption is associated with increased circulating leptin and cholecystokinin, elevated fatty acid oxidation, and 3-beta-hydroxybutyrate ketone levels, and reduced appetite-stimulating neuropeptides, neuropeptide Y and Agouti-related peptide
physiological function
enzyme FBPase is a key rate-controlling enzyme in the gluconeogenic pathway. FBPase activity is regulated synergistically by the allosteric inhibitors AMP and fructose-2,6-bisphosphate. FBPase functions in the degradation of fructose-1,6-bisphosphate, which hydrolyzes to fructose-6-phosphate and phosphate
physiological function
fructose 1,6-bisphosphatase (FBPase) is a major control point in gluconeogenesis, catalyzing the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and phosphate. This step in gluconeogenesis is synergistically downregulated by fructose 2,6-bisphosphate and AMP, which bind to the active site and an allosteric site of FBPase, respectively
physiological function
fructose-1,6-bisphosphatase (FBP1), the rate-limiting enzyme in gluconeogenesis, is a tumor suppressor, especially of breast cancer. The enzyme is commonly upregulated in tumor tissues compared with non-tumor tissues regardless of histological type, and lower FBP1 expression is associated with poor clinical outcome. Genetic silencing of FBP1 reduces aerobic glycolysis and the malignant potential of breast cancer cells. Elevated FBP1 is a critical modulator in breast cancer progression by altering glucose metabolism and the activity of Wnt/ beta-catenin pathway. Mechanism by which FBP1 inhibits tumor progression in breast cancer, overview. The inhibitory effect of FBP1 in glycolysis might be mediated by downregulation of c-Myc
metabolism
fructose-1,6-bisphosphatase (FBPase) catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate and is a key enzyme of gluconeogenesis and glyconeogenesis
metabolism
the enzyme (FBP1) is rate-limiting in gluconeogenes. Its downregulation enhances the activity of Wnt/beta-catenin pathway and increases the level of its downstream targets, including c-Myc and MMP7. Elevated fructose-1,6-bisphosphatase is a critical modulator in breast cancer progression by altering glucose metabolism and the activity of Wnt/beta-Catenin pathway. The enzyme is a tumor suppressor that is frequently down-regulated in cancers, especially breast cancer. Lower FBP1 expression is associated with poor clinical outcome. Up-regulated FBP1 predicts a good prognosis in breast cancer
physiological function
the quaternary structure of isoform FBP2 plays a crucial role in the binding binds to mitochondria where it interacts with proteins involved in regulation of energy homeostasis interaction. The AMP-driven transition of the FBP2 subunit arrangement from active to inactive precludes its association with the mitochondria. Truncation of the evolutionarily conserved N-terminal residues of FBP2 results in a loss of its mitochondria-protective functions
physiological function
the physiological role of muscle FBPase goes beyond its enzymatic function, as this isozyme is localized inside cell nuclei and is shown to interact with mitochondria, where it is involved in regulation of the cell cycle. The behaviour of the muscle isozyme differs greatly from the liver isozyme
additional information
sequence comparisons of human and porcine FBPase 1, overview. The M177 and Y164 interfacial residues are positioned between the AMP-binding site and active sites
additional information
-
sequence comparisons of human and porcine FBPase 1, overview. The M177 and Y164 interfacial residues are positioned between the AMP-binding site and active sites
additional information
-
the FBP active site works by stabilizing the FBPase, and the allosteric site impairs the activity of FBPase through its binding of a nonsubstrate molecule. Competitive inhibition of AMP, fructose 1,6-bisphosphate, or fructose 6-phosphate binding to FBPase with fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP)-binding FBPase
additional information
the transition from the inactive, AMP-associated T state towards the active R state involves a reversible refolding of a key helix that is part of the allosteric centre of muscle FBPase
additional information
-
the transition from the inactive, AMP-associated T state towards the active R state involves a reversible refolding of a key helix that is part of the allosteric centre of muscle FBPase
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). F16P1_HUMAN
338
0
36842
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
additional information
homotetramer
4 * 37000, FBPase is a homotetramer of 222 (D2) symmetry with a major and a minor dimer interface. The dimers connected via the minor interface can rotate with respect to each other, leading to the inactive T-state and active R-state conformations of FBPase. The subunits are labelled C1-C4 and form two functional dimers: C1/C2 and C3/C4. The active site of the C1 subunit is near the C1/C2 interface, while its AMP binding site is near the C1/C4 interface. The C1/C2 and C3/C4 dimers can rotate with respect to each other. Three-dimensional structure analysis, detailed overview. The apoenzyme adopts the active R state
homotetramer
of 222 symmetry with a major and a minor dimer interface. The dimers connected via the minor interface can rotate with respect to each other, leading to the inactive T-state and active R-state conformations
additional information
structure comparisons of human and porcine enzymes, overview. The FBPase pig kidney tetramer overlay of human and pig kidney (PDB IDs 1FTA and 1KZ8, respectively) show nearly identical orientation and conformation in the active site, AMP allosteric binding site, and inhibitor (4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol allosteric binding site architecture
additional information
-
structure comparisons of human and porcine enzymes, overview. The FBPase pig kidney tetramer overlay of human and pig kidney (PDB IDs 1FTA and 1KZ8, respectively) show nearly identical orientation and conformation in the active site, AMP allosteric binding site, and inhibitor (4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol allosteric binding site architecture
additional information
three-dimensional structure analysis of muscle FBPase in its active R state, in the R configuration of muscle FBPase, the C1 subunit has rotated towards the viewer relative to the stationary C3-C4 lower dimer, the three stages of refolding of the N-terminal region of muscle FBPase during the T-to-R transition, overview
additional information
-
three-dimensional structure analysis of muscle FBPase in its active R state, in the R configuration of muscle FBPase, the C1 subunit has rotated towards the viewer relative to the stationary C3-C4 lower dimer, the three stages of refolding of the N-terminal region of muscle FBPase during the T-to-R transition, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are obtained in a micro-batch setup by mixing 0.5 ml volumes of 22.5 mg/ml enzyme in 10 mM potassium/sodium phosphate pH 7.4, 2 mM MnCl2, 5 mM MgCl2, 2 mM ZnCl2, 0.5 mM fructose-2,6-bisphosphate with reservoir solution consisting of 0.1 M Tris-HCl pH 8.5, 2 M ammonium sulfate. Crystal structure of human liver enzyme in the R-state conformation is presented, determined at a resolution of 2.2 A
purified liver FBPase in the R-state conformation, micro-batch method, mixing of 500 nl of 22.5 mg/ml protein in 10 mM potassium/sodium phosphate, pH 7.4, 2 mM MnCl2, 5 mM MgCl2, 2 mM ZnCl2, and 0.5 mM fructose 2,6-bisphosphate, with 500 nl of reservoir solution containing 0.1 M Tris-HCl, pH 8.5, and 2 M ammonium sulfate, X-ray diffraction structure determination and analysis at 2.2 A resolution. Self-Patterson function analysis and various intensity statistics revealed the presence of pseudo-translation and the absence of twinning
crystallization inpresence of 2-propanol, polyethylene glycol and MgCl2 at pH 7.5
-
enzyme in complex with AMP, formycine monophosphate and 5-amino-4-carboxamido-1beta-D-5-phosphate-ribofuranosyl-1H-imidazole
-
hanging-drop vapour-diffusion method at 19°C. The R state of mammalian muscle enzyme (FBPase) is significantly different from the corresponding form of the liver isozyme. T-to-R switch of muscle fructose-1,6-bisphosphatase involves fundamental changes of secondary and quaternary structureMuscle FBPase belongs to the family of proteins containing unstructured, intrinsically disordered elements that adopt a highly ordered structure upon interaction with physiological factors (here after interaction with AMP)
purified muscle FBPase in its active R state, hanging drop vapour diffusion method, mixing of 0.0015 ml of 6 mg/ml protein solution with 0.0015 ml of reservoir solution containing 10 mM Tris buffer pH 7.4, 10 mM MgCl2, 2 M NaCl and 10% v/v PEG 6000, 19°C, 3 months, X-ray diffraction structure determination and analysis at 1.67 A resolution, and purified muscle FBPase in its T state without or with bound AMP, hanging drop vapour diffusion method, mixing of 0.0015 ml of 8 mg/ml protein in 25 mM HEPES, pH 7.0, 2 mM MgCl2, and 0.6 mM AMP, with 0.0015 ml of reservoir solution containing 1.8 M ammonium citrate, 19°C, 3 months, X-ray diffraction structure determination and analysis at 1.84 A and 2.99 A resolution, respectively. Molecular replacement
three-dimensional structure of the human FBPase-2-amino-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole inhibitor complex is solved at 2.0 A resolution, hanging drop method
-
wild-type AMP-bound and product-bound complexes and mutant Q32R, to 1.6 A, 2.2 A, and 2.7 A resolution, respectively. The higher sensitivity of the muscle isozyme towards AMP originates from an additional water-mediated, H-bonded network established between AMP and the binding pocket. The tetrameric assembly of the structures deviates from the canonical R- or T-states, representing novel tetrameric assemblies
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Delta1
-
deletion of the first and the first two N-terminal amino acids of FBPase affects neither the kinetic properties of the enzyme nor its association with aldolase
DELTA10
-
deletion of the first 10 amino acids: affinity to aldolase is significantly reduced, cooperativitiy of Mg2+ activation is abolished and results in biphasic inhibition of the enzyme by AMP. Truncation lowers affinity of muscle FBPase to aldolase about 14times, making it resemble the liver isozyme, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA2
-
deletion of the first and the first two N-terminal amino acids of FBPase affects neither the kinetic properties of the enzyme nor its association with aldolase
DELTA3
-
deletion of the first 3 amino acids: kinetic properties similar to wild-type, affinity to aldolase is significantly reduced, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA4
-
deletion of the first 4 amino acids: kinetic properties similar to wild-type, affinity to aldolase is significantly reduced, mutant shows a lower sensitivity to inhibition by AMP and a little weaker activation by Mg2+, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA5
-
deletion of the first 5 amino acids: mutant is significantly weaker inhibited by AMP than wild-tpye, affinity to aldolase is significantly reduced, kcat and activation by Mg2+ are significantly reduced, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA6
-
deletion of the first 6 amino acids: mutant is significantly weaker inhibited by AMP than wild-tpye, affinity to aldolase is significantly reduced, kcat and activation by Mg2+ are significantly reduced, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA7
-
deletion of the first 7 amino acids: mutant is significantly weaker inhibited by AMP than wild-tpye, affinity to aldolase is significantly reduced, kcat and activation by Mg2+ are significantly reduced, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA8
-
deletion of the first 8 amino acids: mutant is significantly weaker inhibited by AMP than wild-tpye, affinity to aldolase is significantly reduced, kcat significantly reduced, Km (D-fructose 1,6-bisphosphate) similar to wild-type
K203E
-
mutation results in a noticeable drop in the amount of cells having nuclear FBPase
K204E
-
mutation results in a noticeable drop in the amount of cells having nuclear FBPase
K205E
-
mutation results in a noticeable drop in the amount of cells having nuclear FBPase
K207E
-
mutation results in a noticeable drop in the amount of cells having nuclear FBPase
K274L
Q32R
conentration of AMP required for 50% inhibition of the Q32R mutant is increased 19fold, and the cooperativity of both AMP and Mg2+ is abolished or decreased. The mutation affects the conformations of both N-terminal residues and the dynamic loop 5272
additional information
K274L
-
site-directed mutagenesis, active site mutant. The residue K274 is very important for AMP analogue TNP-AMP to bind to the active site of FBPase
K274L
-
equivalent activity to the wild-type enzyme. Wild-type and mutant FBPases behaved identically throughout expression and purification. When the residue K274 is mutated to L274, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate can not bind to the active site, but can bind to the allosteric site
additional information
genetic silencing of fructose-1,6-bisphosphatase (FBP1), FBP1 downregulation enhances the activity of Wnt/beta-catenin pathway and increases the level of its downstream targets, including c-Myc and MMP7
additional information
genetic silencing of fructose-1,6-bisphosphatase (FBP1), FBP1 downregulation enhances the activity of Wnt/beta-catenin pathway and increases the level of its downstream targets, including c-Myc and MMP7
additional information
-
fusion of C-terminal half of Beta vulgaris with C-terminal half of Pisum sativum enzyme, or insertion of cysteine-rich light regulatory sequence of Pisum sativum enzyme into corresponding site of Beta vulgaris enzyme. Both mutants show a decrease in pH-optimum, decrease in sensitivity to AMP, increase in sensitivity to substrate fructose 1,6-bisphosphate
additional information
-
deletion of the first and the first two N-terminal amino acids of FBPase affects neither the kinetic properties of the enzyme not its association with aldolase. The kinetic properties of the mutant with deletion of the first three N-terminal amino acids are entirely the same as these of the wild-type muscle enzyme, its affinity to aldolase is significanltly reduced. The same affinity reduction is observed for the FPase construct lacking the first four N-terminal residues. This protein shows a slight perturbation of its kinetics, a lower sensitivity to inhibition by AMP and a little weaker activation by Mg2+
additional information
-
to determine the role of upregulated liver FBPase in glucose homeostasis human liver FBPase transgenic mice under the control of the transthyretin promoter are generated, expressing the transgene specifically in liver. Hemizygous transgenic mice have an approximately 3fold increase in total liver FBPase mRNA with concomitant increases in FBPase protein and enzyme activity levels. After high-fat feeding, hemizygous transgenics are glucose intolerant compared to wild-type. Homozygous chow-fed transgenic mice show a 5.5fold increase in liver FBPase levels and are glucose intolerant with a significantly higher rate of endogenous glucose production
additional information
-
transgenic mouse lines overexpressing huFBPase gene specifically in pancreatic islet beta-cells are generated to determine whether a specific increase in islet beta-cell FBPase can result in reduced glucose-mediated insulin secretion. FBPase transgenic mice show reduced insulin secretion in response to an intravenous glucose bolus. Pancreatic beta-cell lines (MIN6) stably overexpressing huFBPase show a decreased cell proliferation rate and significantly depressed glucose-induced insulin secretion. These defects are associated with a decrease in the rate of glucose utilization, resulting in reduced cellular ATP levels
additional information
deletion of first 7 N-terminal amino acids of isoform FBP2 markedly impairs colocalization of the enzyme with mitochondria in the presence of GSK3 inhibitor. Deletion of the next 3 residues further enhanced this effect
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
-
half-life of neutral isoenzyme: 710 s, half-life of alkaline isoenzyme: 764 s
additional information
additional information
AMP binding results in improved thermal stability of muscle FBPase
additional information
-
AMP binding results in improved thermal stability of muscle FBPase
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) Rosetta by metal chelating affinity chromatography
recombinant FBPase 1 from Escherichia coli strain BL21(DE3) by anion and cation exchange chromatography, gel filtration, and dialysis
recombinant His6-tagged kidney FBPase from Escherichia coli strain BL21(DE3) by crude cell extract by dialysis and nickel affinity chromatography, cleavage of the His-tag causing low solubility of the human enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene FBP1, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) Rosetta
gene FBP1, sequence comparisons of human and porcine kidney enzymes, recombinant overexpression of C-terminally His6-tagged human kidney FBPase in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain XL-1 Blue supercompetent cells
expression of human fructose-1,6-bisphosphatase in the liver of transgenic mice results in increased glycerol gluconeogenesis
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is up-regulated in tumor tissues compared with non-tumor tissues regardless of histological type
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
upregulated FBP1 predicts a good prognosis in breast cancer, while downregulated FBP1 expression is associated with poor clinical outcome
medicine
drug development
-
the enzyme is a target for drug development in treatment of type 2 diabetes mellitus
medicine
molecular biology
-
promoter methylation is involved in the regulation of expression of both FBPase isoenzymes in normal human tissues as well as in cancer
medicine
AMP site of FBPase may represent a potential drug target for reducing the excessive glucose produced by the gluconeogenesis pathway in patients with type 2 diabetes
medicine
compared with negative littermates, liver-specific FBPase transgenic mice have 50% less adiposity and eat 15% less food but do not have altered energy expenditure. The reduced food consumption is associated with increased circulating leptin and cholecystokinin, elevated fatty acid oxidation, and 3-beta-hydroxybutyrate ketone levels, and reduced appetite-stimulating neuropeptides, neuropeptide Y and Agouti-related peptide
medicine
-
all calcitriol doses increase cancer patient peripheral blood monocyte enzyme activity to normal levels and decrease cytidine deaminase activity to undetectable levels within 48 h, with no significant change in 24-hydrolase activity. Enzyme activity changes are not associated with hypercalcemia
medicine
-
calcitriol treatment-induced increase in FBPase activity in patient peripheral blood monocytes of cancer patients are potential early and sensitive non-hypercalcemia pharmacodynamic measures of calcitriol effects
medicine
-
fructose-1,6-bisphosphatase inhibitors for the treatment of type 2 diabetes
medicine
-
FBP-1 activity in urine as an indicator of damage to renal proximal tubules in children with idiopathic nephrotic syndrome (INS) is investigated. The overload of proximal renal tubules by proteins in children with idiopathic nephrotic syndrome releases FBP-1 into urine. FBP-1 activity in urine may therefore be considered as a marker of damage to the proximal renal tubules in children with idiopathic nephrotic syndrome
medicine
-
FBPase regulates endogenous glucose production and whole body glucose homeostasis in a liver-specific transgenic model. Transgenic mouse can serve as a model for testing human FBPase inhibitor compounds with the potential to treat patients with type 2 diabetes
medicine
-
upregulation of FBPase in pancreatic islet beta-cells, as occurs in states of lipid oversupply and type 2 diabetes, contributes to insulin secretory dysfunction
medicine
-
fructose-1,6-bisphosphatase isoform FBP1 is uniformly depleted in over six hundred clear cell renal cell carcinoma tumors examined. FBP1 antagonizes glycolytic flux in renal tubular epithelial cells, the presumptive clear cell renal cell carcinoma cell of origin, thereby inhibiting a potential Warburg effect. In addition, in von Hippel-Lindau protein-deficient clear cell renal cell carcinoma cells, FBP1 restrains cell proliferation, glycolysis and the pentose phosphate pathway in a catalytic activity-independent manner, by inhibiting nuclear hypoxia-inducible factor function via direct interaction with the hypoxia-inducible factor inhibitory domain
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dzugaj, A.; Kochman, M.
Purification of human liver fructose-1,6-bisphosphatase
Biochim. Biophys. Acta
614
407-412
1980
Homo sapiens
Skalecki, K.; Rakus, D.; Wisniewski, J.R.; Kolodziej, J.; Dzugaj, A.
cDNA sequence and kinetic properties of human lung fructose(1,6)bisphosphatase
Arch. Biochem. Biophys.
365
1-9
1999
Homo sapiens (P09467)
Iversen, L.F.; Brzozowski, M.; Hastrup, S.; Hubbard, R.; Kastrup, J.S.; Larsen, I.K.; Naerum, L.; Norskov-Lauridsen, L.; Rasmussen, P.B.; Thim, L.; Wiberg, F.C.; Lundgren, K.
Characterization of the allosteric binding pocket of human liver fructose-1,6-bisphosphatase by protein crystallography and inhibitor activity studies
Protein Sci.
6
971-982
1997
Homo sapiens
Skalecki, K.; Mularczyk, W.; Dzugaj, A.
Kinetic properties of D-fructose-1,6-bisphosphate 1-phosphohydrolase isolated from human muscle
Biochem. J.
310
1029-1035
1995
Homo sapiens
Adams, A.; Redden, C.; Menahem, S.
Characterization of human fructose 1,6-bisphosphatase in control and deficient tissues
J. Inherit. Metab. Dis.
13
829-848
1990
Homo sapiens
Koekemoer, T.C.; Stanton, L.A.; Oelofsen, W.
Kinetic properties of ovine adipose tissue fructose-1,6-bisphosphatase
Comp. Biochem. Physiol. B
109
443-450
1994
Oryctolagus cuniculus, Ovis aries, Homo sapiens, Rattus norvegicus
-
Zhu, D.W.; Xu, G.J.; Rehse, P.H.; Shi, R.; Zhao, F.K.; Lin, S.X.
Crystallization and preliminary crystallographic data of fructose-1,6-bisphosphatase from human muscle
Acta Crystallogr. Sect. D
57
847-849
2001
Homo sapiens
Zhang, F.W.; Zhao, F.K.; Xu, G.J.
Molecular cloning, expression and purification of muscle fructose-1,6-bisphosphatase from Zaocys dhumnades: the role of the N-terminal sequence in AMP activation at alkaline pH
Biol. Chem.
381
561-566
2000
Homo sapiens, Rattus norvegicus, Sus scrofa, Ptyas dhumnades
Wright, S.W.; Hageman, D.L.; McClure, L.D.; Carlo, A.A.; Treadway, J.L.; Mathiowetz, A.M.; Withka, J.M.; Bauer, P.H.
Allosteric inhibition of fructose-1,6-bisphosphatase by anilinoquinazolines
Bioorg. Med. Chem. Lett.
11
17-21
2001
Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
Rakus, D.; Skalecki, K.; Dzugaj, A.
Kinetic properties of pig (Sus scrofa domestica) and bovine (Bos taurus) D-fructose-1,6-bisphosphate 1-phosphohydrolase (F1,6BPase): liver-like isozymes in mammalian lung tissue
Comp. Biochem. Physiol. B
127
123-134
2000
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Sus scrofa domesticus
Gizak, A.; Rakus, D.; Kolodziej, J.; Zabel, M.; Ogorzalek, A.; Dzugaj, A.
Human lung fructose-1,6-bisphosphatase is localized in pneumocytes II
Histol. Histopathol.
16
53-55
2001
Homo sapiens
Gizak, A.; Rakus, D.; Dzugaj, A.
Immunohistochemical localization of human fructose-1,6-bisphosphatase in subcellular structures of myocytes
Histol. Histopathol.
18
135-142
2003
Homo sapiens
von Geldern, T.W.; Lai, C.; Gum, R.J.; Daly, M.; Sun, C.; Fry, E.H.; Abad-Zapatero, C.
Benzoxazole benzenesulfonamides are novel allosteric inhibitors of fructose-1,6-bisphosphatase with a distinct binding mode
Bioorg. Med. Chem. Lett.
16
1811-1815
2006
Homo sapiens
Muindi, J.R.; Peng, Y.; Wilson, J.W.; Johnson, C.S.; Branch, R.A.; Trump, D.L.
Monocyte fructose 1,6-bisphosphatase and cytidine deaminase enzyme activities: potential pharmacodynamic measures of calcitriol effects in cancer patients
Cancer Chemother. Pharmacol.
59
97-104
2006
Homo sapiens
Rakus, D.; Maciaszczyk, E.; Wawrzycka, D.; Ulaszewski, S.; Eschrich, K.; Dzugaj, A.
The origin of the high sensitivity of muscle fructose 1,6-bisphosphatase towards AMP
FEBS Lett.
579
5577-5581
2005
Homo sapiens (P09467)
Yanez, A.J.; Bertinat, R.; Spichiger, C.; Carcamo, J.G.; de Los Angeles Garcia, M.; Concha, II; Nualart, F.; Slebe, J.C.
Novel expression of liver FBPase in Langerhans islets of human and rat pancreas
J. Cell. Physiol.
205
19-24
2005
Homo sapiens, Rattus norvegicus
Cazalis, R.; Chueca, A.; Sahrawy, M.; Lopez-Gorge, J.
Construction of chimeric cytosolic fructose-1,6-bisphosphatases by insertion of a chloroplastic redox regulatory cluster
J. Physiol. Biochem.
60
7-22
2004
Beta vulgaris, Homo sapiens
Lai, C.; Gum, R.J.; Daly, M.; Fry, E.H.; Hutchins, C.; Abad-Zapatero, C.; von Geldern, T.W.
Benzoxazole benzenesulfonamides as allosteric inhibitors of fructose-1,6-bisphosphatase
Bioorg. Med. Chem. Lett.
16
1807-1810
2006
Homo sapiens, Rattus norvegicus
Sybirna, N.; Dziewulska-Szwajkowska, D.; Barska, M.; Dzugaj, A.
Mononuclear and polymorphonuclear leukocytes show increased fructose-1,6-bisphosphatase activity in patients with type 1 diabetes mellitus
Cell Biol. Int.
30
624-630
2006
Homo sapiens
van Poelje, P.D.; Dang, Q.; Erion, M.D.
Discovery of fructose-1,6-bisphosphatase inhibitors for the treatment of type 2 diabetes
Curr. Opin. Drug Discov. Devel.
10
430-437
2007
Homo sapiens
Lamont, B.J.; Visinoni, S.; Fam, B.C.; Kebede, M.; Weinrich, B.; Papapostolou, S.; Massinet, H.; Proietto, J.; Favaloro, J.; Andrikopoulos, S.
Expression of human fructose-1,6-bisphosphatase in the liver of transgenic mice results in increased glycerol gluconeogenesis
Endocrinology
147
2764-2772
2006
Homo sapiens
Erion, M.D.; Dang, Q.; Reddy, M.R.; Kasibhatla, S.R.; Huang, J.; Lipscomb, W.N.; van Poelje, P.D.
Structure-guided design of AMP mimics that inhibit fructose-1,6-bisphosphatase with high affinity and specificity
J. Am. Chem. Soc.
129
15480-15490
2007
Homo sapiens (P09467), Homo sapiens
Dang, Q.; Kasibhatla, S.R.; Reddy, K.R.; Jiang, T.; Reddy, M.R.; Potter, S.C.; Fujitaki, J.M.; van Poelje, P.D.; Huang, J.; Lipscomb, W.N.; Erion, M.D.
Discovery of potent and specific fructose-1,6-bisphosphatase inhibitors and a series of orally-bioavailable phosphoramidase-sensitive prodrugs for the treatment of type 2 diabetes
J. Am. Chem. Soc.
129
15491-15502
2007
Homo sapiens, Rattus norvegicus
Mutyala, R.; Reddy, R.N.; Sumakanth, M.; Reddanna, P.; Reddy, M.R.
Calculation of relative binding affinities of fructose 1,6-bisphosphatase mutants with adenosine monophosphate using free energy perturbation method
J. Comput. Chem.
28
932-937
2007
Homo sapiens
Gizak, A.; Maciaszczyk, E.; Dzugaj, A.; Eschrich, K.; Rakus, D.
Evolutionary conserved N-terminal region of human muscle fructose 1,6-bisphosphatase regulates its activity and the interaction with aldolase
Proteins
72
209-216
2008
Homo sapiens
Visinoni, S.; Fam, B.C.; Blair, A.; Rantzau, C.; Lamont, B.J.; Bouwman, R.; Watt, M.J.; Proietto, J.; Favaloro, J.M.; Andrikopoulos, S.
Increased glucose production in mice overexpressing human fructose-1,6-bisphosphatase in the liver
Am. J. Physiol. Endocrinol. Metab.
295
E1132-E1141
2008
Homo sapiens
Bigl, M.; Jandrig, B.; Horn, L.C.; Eschrich, K.
Aberrant methylation of human L- and M-fructose 1,6-bisphosphatase genes in cancer
Biochem. Biophys. Res. Commun.
377
720-724
2008
Homo sapiens
Kepka, A.; Dariusz Szajda, S.; Stypu?kowska, A.; Waszkiewicz, N.; Jankowska, A.; Chojnowska, S.; Zwierz, K.
Urinary fructose-1,6-bisphosphatase activity as a marker of the damage to the renal proximal tubules in children with idiopathic nephrotic syndrome
Clin. Chem. Lab. Med.
46
831-835
2008
Homo sapiens
Kebede, M.; Favaloro, J.; Gunton, J.E.; Laybutt, D.R.; Shaw, M.; Wong, N.; Fam, B.C.; Aston-Mourney, K.; Rantzau, C.; Zulli, A.; Proietto, J.; Andrikopoulos, S.
Fructose-1,6-bisphosphatase overexpression in pancreatic beta-cells results in reduced insulin secretion: a new mechanism for fat-induced impairment of beta-cell function
Diabetes
57
1887-1895
2008
Homo sapiens
Dang, Q.; Kasibhatla, S.R.; Jiang, T.; Fan, K.; Liu, Y.; Taplin, F.; Schulz, W.; Cashion, D.K.; Reddy, K.R.; van Poelje, P.D.; Fujitaki, J.M.; Potter, S.C.; Erion, M.D.
Discovery of phosphonic diamide prodrugs and their use for the oral delivery of a series of fructose 1,6-bisphosphatase inhibitors
J. Med. Chem.
51
4331-4339
2008
Homo sapiens, Rattus norvegicus
Tsukada, T.; Takahashi, M.; Takemoto, T.; Kanno, O.; Yamane, T.; Kawamura, S.; Nishi, T.
Synthesis, SAR, and X-ray structure of tricyclic compounds as potent FBPase inhibitors
Bioorg. Med. Chem. Lett.
19
5909-5912
2009
Homo sapiens (P09467), Homo sapiens
Gizak, A.; Maciaszczyk-Dziubinska, E.; Jurowicz, M.; Rakus, D.
Muscle FBPase is targeted to nucleus by its 203KKKGK207 sequence
Proteins
77
262-267
2009
Homo sapiens
Hebeisen, P.; Haap, W.; Kuhn, B.; Mohr, P.; Wessel, H.P.; Zutter, U.; Kirchner, S.; Ruf, A.; Benz, J.; Joseph, C.; Alvarez-Sanchez, R.; Gubler, M.; Schott, B.; Benardeau, A.; Tozzo, E.; Kitas, E.
Orally active aminopyridines as inhibitors of tetrameric fructose-1,6-bisphosphatase
Bioorg. Med. Chem. Lett.
21
3237-3242
2011
Homo sapiens, Mus musculus
Dang, Q.; Kasibhatla, S.R.; Xiao, W.; Liu, Y.; Dare, J.; Taplin, F.; Reddy, K.R.; Scarlato, G.R.; Gibson, T.; van Poelje, P.D.; Potter, S.C.; Erion, M.D.
Fructose-1,6-bisphosphatase Inhibitors. 2. Design, synthesis, and structure-activity relationship of a series of phosphonic acid containing benzimidazoles that function as 5-adenosinemonophosphate (AMP) mimics
J. Med. Chem.
53
441-451
2010
Homo sapiens, Rattus norvegicus
Dang, Q.; Liu, Y.; Cashion, D.K.; Kasibhatla, S.R.; Jiang, T.; Taplin, F.; Jacintho, J.D.; Li, H.; Sun, Z.; Fan, Y.; Dare, J.; Tian, F.; Li, W.; Gibson, T.; Lemus, R.; van Poelje, P.D.; Potter, S.C.; Erion, M.D.
Discovery of a series of phosphonic Acid-containing thiazoles and orally bioavailable diamide prodrugs that lower glucose in diabetic animals through inhibition of fructose-1,6-bisphosphatase
J. Med. Chem.
54
153-165
2011
Homo sapiens
Bie, J.; Liu, S.; Zhou, J.; Xu, B.; Shen, Z.
Design, synthesis and biological evaluation of 7-nitro-1H-indole-2-carboxylic acid derivatives as allosteric inhibitors of fructose-1,6-bisphosphatase
Bioorg. Med. Chem.
22
1850-1862
2014
Homo sapiens
Visinoni, S.; Khalid, N.F.; Joannides, C.N.; Shulkes, A.; Yim, M.; Whitehead, J.; Tiganis, T.; Lamont, B.J.; Favaloro, J.M.; Proietto, J.; Andrikopoulos, S.; Fam, B.C.
The role of liver fructose-1,6-bisphosphatase in regulating appetite and adiposity
Diabetes
61
1122-1132
2012
Homo sapiens (P09467)
Liao, B.R.; He, H.B.; Yang, L.L.; Gao, L.X.; Chang, L.; Tang, J.; Li, J.Y.; Li, J.; Yang, F.
Synthesis and structure-activity relationship of non-phosphorus-based fructose-1,6-bisphosphatase inhibitors: 2,5-diphenyl-1,3,4-oxadiazoles
Eur. J. Med. Chem.
83
15-25
2014
Homo sapiens
Pirog, M.; Gizak, A.; Rakus, D.
Changes in quaternary structure of muscle fructose-1,6-bisphosphatase regulate affinity of the enzyme to mitochondria
Int. J. Biochem. Cell Biol.
48
55-59
2014
Homo sapiens (O00757)
Li, B.; Qiu, B.; Lee, D.S.; Walton, Z.E.; Ochocki, J.D.; Mathew, L.K.; Mancuso, A.; Gade, T.P.; Keith, B.; Nissim, I.; Simon, M.C.
Fructose-1,6-bisphosphatase opposes renal carcinoma progression
Nature
513
251-255
2014
Homo sapiens
Shi, R.; Chen, Z.Y.; Zhu, D.W.; Li, C.; Shan, Y.; Xu, G.; Lin, S.X.
Crystal structures of human muscle fructose-1,6-bisphosphatase: novel quaternary states, enhanced AMP affinity, and allosteric signal transmission pathway
PLoS ONE
8
e71242
2013
Homo sapiens (O00757), Homo sapiens
Rakus, D.; Gizak, A.; Kasprzak, A.A.; Zarzycki, M.; Maciaszczyk-Dziubinska, E.; Dzugaj, A.
The mechanism of calcium-induced inhibition of muscle fructose 1,6-bisphosphatase and destabilization of glyconeogenic complex
PLoS ONE
8
e76669
2013
Homo sapiens
Ruf, A.; Tetaz, T.; Schott, B.; Joseph, C.; Rudolph, M.
Quadruple space-group ambiguity owing to rotational and translational noncrystallographic symmetry in human liver fructose-1,6-bisphosphatase
Acta Crystallogr. Sect. D
72
1212-1224
2016
Homo sapiens (P09467), Homo sapiens
Barciszewski, J.; Wisniewski, J.; Kolodziejczyk, R.; Jaskolski, M.; Rakus, D.; Dzugaj, A.
T-to-R switch of muscle fructose-1,6-bisphosphatase involves fundamental changes of secondary and quaternary structure
Acta Crystallogr. Sect. D
72
536-550
2016
Homo sapiens (O00757), Homo sapiens
Li, K.; Ying, M.; Feng, D.; Du, J.; Chen, S.; Dan, B.; Wang, C.; Wang, Y.
Fructose-1,6-bisphosphatase is a novel regulator of Wnt/beta-catenin pathway in breast cancer
Biomed. Pharmacother.
84
1144-1149
2016
Homo sapiens (O00757), Homo sapiens (P09467)
Topaz, G.R.; Epiter-Smith, V.; Robolo, C.; Emad, M.; Ford, V.; Daley, J.; Byron, J.; Stieglitz, K.A.
Characterization of recombinant fructose 1,6-bisphosphatase (FBPase) gene mutations evidence of inhibition/activation of FBPase protein by gene mutation
Biosci. Rep.
39
BSR20180960
2019
Sus scrofa (P00636), Homo sapiens (P09467), Homo sapiens
Bie, J.; Liu, S.; Li, Z.; Mu, Y.; Xu, B.; Shen, Z.
Discovery of novel indole derivatives as allosteric inhibitors of fructose-1,6-bisphosphatase
Eur. J. Med. Chem.
90
394-405
2015
Homo sapiens, Homo sapiens (P09467)
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