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Information on EC 3.1.3.11 - fructose-bisphosphatase
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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
- chloroplast
- phosphoenolpyruvate
-
carboxykinase
- glucose-6-phosphatase
- glycogen
-
phosphofructokinase
- hexokinase
- 2,6-bisphosphate
- spinach
- malate
- thioredoxins
- starch
- co2
- fructose-2,6-bisphosphate
-
6-phosphatase
- glucokinase
- pentose
-
analbuminemic
- pepck
- glucagon
- fructose-6-phosphate
- 3-phosphoglycerate
- g6pase
- ribulose-1,5-bisphosphate
-
nadp-malate
-
calvin
-
light-dependent
-
amp-dependent
- oleracea
- sedoheptulose
- triose
- rubisco
- dihydroxyacetone
- ribulose
- phosphoribulokinase
-
t-states
-
light-activated
-
antihyperglycemic
-
sucrose-phosphate
- trx
-
phytolacca
- 6-phosphofructo-1-kinase
-
triose-phosphate
- synthesis
-
4.1.1.39
- medicine
- biotechnology
-
2.7.1.11
- drug development
- molecular biology
-
monophosphatase
- ribulose-5-phosphate
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
fructose-1,6-bisphosphatase, fructose 1,6-bisphosphatase, fructose bisphosphatase, fructose diphosphatase, fructose 1,6-diphosphatase, fbp-1, fru-1,6-p2ase, cfbpase, fructose 1,6-biphosphatase, hexose diphosphatase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
archaeal FBP aldolase/phosphatase
archaeal-like fructose-1,6-bisphosphatase
beta-PGM
CFBPase
class II FBPase
class II fructose-1,6-bisphosphatase
CY-F1
-
-
-
-
D-fructose 1,6-bisphosphatase
D-fructose 1,6-diphosphatase
-
-
-
-
D-fructose-1,6-bisphosphatase
-
-
-
-
D-fructose-1,6-bisphosphate 1-phosphohydrolase
-
-
-
-
D-fructose-1,6-bisphosphate phosphatase
-
-
-
-
FBP aldolase/phosphatase
FBP-1
FBPase
FBPase II
FBPase IV
the enzyme is present in euryarchaeal and hyperthermophilic bacterial species
Fru-1,6-P2ase
fructose 1,6-bisphosphatase
fructose 1,6-bisphosphatase II
fructose 1,6-bisphosphate 1-phosphatase
-
-
-
-
fructose 1,6-bisphosphate phosphatase
-
-
-
-
fructose 1,6-diphosphatase
-
-
-
-
fructose 1,6-diphosphate phosphatase
-
-
-
-
fructose bisphosphatase
fructose bisphosphate phosphatase
-
-
-
-
fructose diphosphatase
-
-
-
-
fructose diphosphate phosphatase
-
-
-
-
fructose-1,6-bisphosphatase
fructose-1,6-bisphosphate (FBP) aldolase/phosphatase
EC 4.1.2.13/EC 3.1.3.11. A bifunctional, thermostable enzyme that catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages
fructose-1,6-bisphosphate aldolase/phosphatase
GlpX
GlpXp
hexose bisphosphatase
-
-
-
-
hexose diphosphatase
-
-
-
-
hexosediphosphatase
-
-
-
-
RAE-30
-
-
-
-
slr2094
STK_03180
locus name. The bifunctional enzyme also shows activity of EC 4.1.2.13
additional information
YK23 is a member of the histidine phosphatase (phosphoglyceromutase) superfamily
archaeal-like fructose-1,6-bisphosphatase
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q5SJM8
-
-
FBP aldolase/phosphatase
EC 4.1.2.13/EC 3.1.3.11. A bifunctional, thermostable enzyme that catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages
FBP aldolase/phosphatase
bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13
FBP aldolase/phosphatase
bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13
-
FBPase
-
-
-
-
Fru-1,6-P2ase
-
-
-
-
fructose 1,6-bisphosphatase
-
-
-
-
fructose-1,6-bisphosphate aldolase/phosphatase
EC 4.1.2.13/EC 3.1.3.11. A bifunctional, thermostable enzyme that catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages
fructose-1,6-bisphosphate aldolase/phosphatase
bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
uni-bi mechanism in forward direction
-
D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
uni-bi mechanism
-
D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
steady state ordered uni bi mechanism
-
D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
all four subunits are active in a single turnover event
-
D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
the chloroplast enzyme of higher plants can occur in an active form that is inactivated upon disulfide bridge formation between Cys155 and Cys174
-
D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
loop 52-72 is an essential element in the allosteric mechanism of enzyme
-
D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
in supramolecular complex with alpha-actinin and aldolase, D-fructose 1,6-bisphosphate is transferred directly from aldolase to enzyme without mixing with the bulk phase
-
D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
D-fructose-1,6-bisphosphate 1-phosphohydrolase
The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
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CAS REGISTRY NUMBER
COMMENTARY
9001-52-9
-
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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-glucose 1,6-bisphosphate + H2O
D-glucose 6-phosphate + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
23% of the activity found with D-fructose 1,6-bisphosphate
-
?
glucose 1,6-diphosphate + H2O
?
-
about 10% of maximal activity
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
?
ribulose 1,5-bisphosphate + H2O
ribulose 5-phosphate + phosphate
15% of activity obtained with D-fructose 1,6-bisphosphate
-
?
beta-D-glucose 1,6-bisphosphate + H2O
D-glucose 6-phosphate + phosphate
-
-
-
-
?
beta-D-glucose 1,6-bisphosphate + H2O
D-glucose 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
-
-
-
-
?
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
G7YVB4
-
-
-
?
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
-
Fbp plays a key role in gluconeogenesis that supplies cellular building blocks such as hexose and intermediates of the pentose phosphate pathway for cell growth. Fructose-1,6-bisphosphatase increases its abundance by 2.0-2.7fold on various aromatic compounds. Fbp plays a key role in aromatic assimilation by Coryneacterium glutamicum. The Fbp gene is disrupted and the mutant WTDfbp loses the ability to grow on aromatic compounds. Genetic complementation by the Fbp gene restores this ability
-
-
?
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
best substrate
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
enzyme functions with FBPase I in the centarle pathways of carbohydrate metabolism
-
?
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
-
-
-
-
?
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 a part of Calvin cycle
-
?
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-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is highly specific for D-fructose 1,6-bisphosphate. At 1 mM substrate, activity is only 40% of the activity at 0.06 mM substrate
-
-
?
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
the the chloroplastic isozyme plays a key role in the Calvin cycle and the cytoplasmic isozyme plays a key role in the sucrose synthesis in cytoplasm
-
?
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
the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis. It catalyses a multi-step reaction by remodelling its active site according to the respective catalytic requirements
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis. It catalyses a multi-step reaction by remodelling its active site according to the respective catalytic requirements
-
-
?
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
-
regulatory enzyme of glyconeogenesis. FBPase participates in some nuclear processes during development and regeneration of skeletal muscle
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
the coregulation of phosphofructo 1-kinase I and fructose 1,6-bisphosphatase are required for the ability of these cells to respond to glucose and induce metabolic and Ca2+ signals that can be important for sperm development and function
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
best substrate
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the substrate is bound in its linear, open conformation with the cleavable C1-phosphate positioned deep in the active site
-
-
?
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
the bifunctional enzyme also shows activity of EC 4.1.2.13. The crystal structures of the enzyme in the two forms reveals that it achieves its bifunctionality by transforming its active-site architecture, through the toggle switch-like motions of the three mobile loop regions
-
-
r
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the bifunctional enzyme also shows activity of EC 4.1.2.13. The crystal structures of the enzyme in the two forms reveals that it achieves its bifunctionality by transforming its active-site architecture, through the toggle switch-like motions of the three mobile loop regions
-
-
r
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
-
-
-
?
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
FBPase contributes to the partitioning of the fixed carbon for ribulose-1,5-bisphosphate regeneration or starch synthesis
-
-
?
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
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
best substrate
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Q5SJM8
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q5SJM8
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
the enzyme plays a key role in the Calvin cycle
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
key regulatory enzyme in the control of the Emden-Meyerhof pathway
-
-
-
D-fructose 1,6-diphosphate + H2O
?
-
key regulatory enzyme in the control of the Emden-Meyerhof pathway
-
-
-
D-fructose 1,6-diphosphate + H2O
?
-
the enzyme is involved in the futile cycling of fructose 6-phosphate and fructose 1,6-diphosphate in flight muscle, the net result of which is the hydrolysis of ATP
-
-
-
D-fructose 1,6-diphosphate + H2O
?
-
enzyme plays a key regulatory role in the futile cycle of fructose 1,6-diphosphate synthesis and degradation
-
-
-
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-diphosphate + H2O
?
-
regulatory enzyme in gluconeogenesis
-
-
-
D-fructose 1,6-diphosphate + H2O
?
-
enzyme is involved in photosynthetic process
-
-
-
D-fructose 1,6-diphosphate + H2O
?
-
isoenzyme A is present when the organism is grown under autotrophic conditions but is not synthesized during heterotrophic growth. Isoenzyme B is detected in both autothrophically and heterotrophically grown organisms
-
-
-
D-fructose 1,6-diphosphate + H2O
?
-
the enzyme may be involved in the regulation of the Calvin-Bassham carbon reduction cycle
-
-
-
D-fructose 1,6-diphosphate + H2O
?
-
key regulatory enzyme in carbohydrate synthesis in both gluconeogenesis and photosynthesis
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
r
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
r
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
-
-
-
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
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
-
-
-
?
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
-
enzyme is a part of Calvin cycle
-
?
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
-
-
-
?
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
-
-
-
?
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
-
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 6-phosphate + phosphate
D-fructose 1,6-diphosphate + H2O
-
-
-
r
ribulose 1,5-diphosphate + H2O
?
-
23% of the activity with fructose 1,6-diphosphate
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
no activity
-
-
-
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
intestinal and muscle enzyme
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
81% of the activity with fructose 1,6-diphosphate
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
at 22.4% of the activity with fructose 1,6-diphosphate
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
about 5% of maximal activity
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
no activity
-
-
-
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
-
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
activity with isoenzyme F-1, no activity with isoenzyme F-II
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
no activity
-
-
-
additional information
?
-
-
role as a key enzyme in CO2 assimilation and also in coordinating carbon and nitrogen metabolism
-
-
-
additional information
?
-
-
bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
-
-
-
additional information
?
-
-
the chromosome-encoded isoform is the major fructose 1,6-bisphosphatase of Bacillus methanolicus
-
-
-
additional information
?
-
the chromosome-encoded isoform is the major fructose 1,6-bisphosphatase of Bacillus methanolicus
-
-
-
additional information
?
-
Q6TV42
the chromosome-encoded isoform is the major fructose 1,6-bisphosphatase of Bacillus methanolicus
-
-
-
additional information
?
-
the chromosome-encoded isoform is the major fructose 1,6-bisphosphatase of Bacillus methanolicus
-
-
-
additional information
?
-
Q6TV42
the chromosome-encoded isoform is the major fructose 1,6-bisphosphatase of Bacillus methanolicus
-
-
-
additional information
?
-
-
bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
-
-
-
additional information
?
-
-
enzyme together with phosphofructokinase plays a crucial role in metabolism of pancreatic islet cells
-
-
-
additional information
?
-
-
bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
-
-
-
additional information
?
-
-
no substrate: D-glucose 1-phosphate, D-glucose 6-phosphate, sorbitol 6-phosphate, phosphoenolpyruvate, D-fructose 6-phosphate, 3-glycerate phosphate, dihydroxyacetone
-
-
-
additional information
?
-
-
enzyme together with phosphofructokinase plays a crucial role in metabolism of pancreatic islet cells
-
-
-
additional information
?
-
-
enzyme influences the connection between DNA damage, aging and oxidative stress
-
-
-
additional information
?
-
purified YK23 exhibits high phosphatase activity against fructose 1,6-bisphosphate, significant hydrolytic activity toward fructose 1-phosphate, and detectable activity with glyceraldehyde 3-phosphate, erythrose 4-phosphate, and ribulose 1,5-diphosphate
-
-
-
additional information
?
-
-
binding of the first substrate molecule, in one dimer of the enzyme, produces a conformational change at the other dimer, reducing the substrate affinity and catalytic activity of its subunits
-
-
-
additional information
?
-
not: D-fructose 1-phosphate, D-fructose 6-phosphate, D-fructose 2,6-bisphosphate, glycerol 3-phosphate, glycerol 1-phosphate
-
?
additional information
?
-
-
not: D-fructose 1-phosphate, D-fructose 6-phosphate, D-fructose 2,6-bisphosphate, glycerol 3-phosphate, glycerol 1-phosphate
-
?
additional information
?
-
-
the enzyme TNA1-Fbp has broad substrate specificities for D-fructose-1,6-bisphosphate and its analogues including D-fructose 1-bisphosphate, D-fructose 6-phosphate, D-glucose 1-phosphate, D-glucose 6-phosphate, glycerol 2-phosphate, and phosphoenolpyruvate, as well as AMP, ADP ATP, substrate specificity, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-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
-
-
-
-
?
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
-
Fbp plays a key role in gluconeogenesis that supplies cellular building blocks such as hexose and intermediates of the pentose phosphate pathway for cell growth. Fructose-1,6-bisphosphatase increases its abundance by 2.0-2.7fold on various aromatic compounds. Fbp plays a key role in aromatic assimilation by Coryneacterium glutamicum. The Fbp gene is disrupted and the mutant WTDfbp loses the ability to grow on aromatic compounds. Genetic complementation by the Fbp gene restores this ability
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
P0A9C9
enzyme functions with FBPase I in the centarle pathways of carbohydrate metabolism
-
?
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
Q95AJ2
enzyme is a part of Calvin cycle
-
?
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-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
Q8RW99
the the chloroplastic isozyme plays a key role in the Calvin cycle and the cytoplasmic isozyme plays a key role in the sucrose synthesis in cytoplasm
-
?
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
B1YAL1
the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
B1YAL1
the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Q8TZH9
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
regulatory enzyme of glyconeogenesis. FBPase participates in some nuclear processes during development and regeneration of skeletal muscle
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
the coregulation of phosphofructo 1-kinase I and fructose 1,6-bisphosphatase are required for the ability of these cells to respond to glucose and induce metabolic and Ca2+ signals that can be important for sperm development and function
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
P36136
best substrate
-
-
?
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
Q59943
FBPase contributes to the partitioning of the fixed carbon for ribulose-1,5-bisphosphate regeneration or starch synthesis
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Q8NKR9
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
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
Q5SJM8
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q5SJM8
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
the enzyme plays a key role in the Calvin cycle
-
?
D-fructose 1,6-diphosphate + H2O
?
-
key regulatory enzyme in the control of the Emden-Meyerhof pathway
-
-
-
D-fructose 1,6-diphosphate + H2O
?
-
key regulatory enzyme in the control of the Emden-Meyerhof pathway
-
-
-
D-fructose 1,6-diphosphate + H2O
?
-
the enzyme is involved in the futile cycling of fructose 6-phosphate and fructose 1,6-diphosphate in flight muscle, the net result of which is the hydrolysis of ATP
-
-
-
D-fructose 1,6-diphosphate + H2O
?
-
enzyme plays a key regulatory role in the futile cycle of fructose 1,6-diphosphate synthesis and degradation
-
-
-
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-diphosphate + H2O
?
-
regulatory enzyme in gluconeogenesis
-
-
-
D-fructose 1,6-diphosphate + H2O
?
-
enzyme is involved in photosynthetic process
-
-
-
D-fructose 1,6-diphosphate + H2O
?
-
isoenzyme A is present when the organism is grown under autotrophic conditions but is not synthesized during heterotrophic growth. Isoenzyme B is detected in both autothrophically and heterotrophically grown organisms
-
-
-
D-fructose 1,6-diphosphate + H2O
?
-
the enzyme may be involved in the regulation of the Calvin-Bassham carbon reduction cycle
-
-
-
D-fructose 1,6-diphosphate + H2O
?
-
key regulatory enzyme in carbohydrate synthesis in both gluconeogenesis and photosynthesis
-
-
-
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is a part of Calvin cycle
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
additional information
?
-
-
role as a key enzyme in CO2 assimilation and also in coordinating carbon and nitrogen metabolism
-
-
-
additional information
?
-
-
bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
-
-
-
additional information
?
-
-
bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
-
-
-
additional information
?
-
-
enzyme together with phosphofructokinase plays a crucial role in metabolism of pancreatic islet cells
-
-
-
additional information
?
-
-
bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
-
-
-
additional information
?
-
-
enzyme together with phosphofructokinase plays a crucial role in metabolism of pancreatic islet cells
-
-
-
additional information
?
-
-
enzyme influences the connection between DNA damage, aging and oxidative stress
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cu2+
G7YVB4
stimulation increases in the order Mg2+, Mn2+, Zn2+, Cu2+. Mg2+ stimulates below 5 mM, inhibits above 10 mM
Hg2+
low concentrations stimulate the oxidized enzyme form, but not the reduced enzyme form many hundred-fold. Half-maximal stimulation at 0.2 femtoM: Hg2+ stimulates by binding to an enzyme thiol group, thereby stabilizing the oxidized enzyme in an active conformation
K+
KCl
Mg2+
Mn2+
Na+
Tl+
Zn2+
additional information
Ca2+
-
regulation of complex of enzyme with alodolase. Elevated Ca2+ concentration decreases association constant of enzyme-aldolase complex and enzyme-alpha-actinin complex. Release of Ca2+ during muscle contraction may result in inhibition of glyconeogenesis and in the acceleration of glycolysis
K+
-
inhibitory in the cytosol, activating in mitochondria and microsomes, depedent on the presence of Mg2+ or Mn2+, overview
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+
-
required at different concentrations in the different subcellular fractions, overview
Mg2+
G7YVB4
stimulation increases in the order Mg2+, Mn2+, Zn2+, Cu2+. Mg2+ stimulates below 5 mM, inhibits above 10 mM
Mg2+
-
absolute requirement for divalent metal ion is best satisfied by 1 mM Mg2+
Mg2+
wild-type muscle enzyme, Hill coefficient 1.89, wild-type liver enzyme, hill coefficient 1.83
Mg2+
-
divalent cation required. Mn2+ or Mg2+; optimal concentration at pH 7.5: 1-1.5 mM
Mg2+
-
divalent cation required. Mn2+ or Mg2+; optimal concentration: 1-1.5 mM
Mg2+
-
in the methanococcal extracts, activity is dependent on MgCl2 and cysteine
Mg2+
-
inhibitory at higher concentration on free enzyme. Not inhibitory for enzyme in complex with aldolase. Mg2+ at physiological concentration increases the affinity of enzyme to aldolase, at higher concentration decreases the concentration of the complex
Mg2+
-
divalent cation required. Mn2+ or Mg2+; Km: 3.3 mM; only 27% of the maximal activity observed with Mn2+
Mg2+
-
the oxidized wild-type enzyme is active only at very high Mg2+ concentrations, the Mg2+ requirement of oxidized and reduced forms of wild-type and mutant enzymes is compared. The reduction of the regulatory disulfide has a positive allosteric effect on the binding of the catalytically essential Mg2+ in the active site.
Mg2+
-
required, comparison of activities of wild-type and mutant enzymes in dependence of Mg2+ concentrations
Mg2+
-
comparison of activity at 2, 10 and 15 mM Mg2+ of native and two recombinant enzymes
Mg2+
-
absolute requirement for divalent cation, fulfilled by Mg2+, Zn2+, Mn2+, maximum activity at 5 mM. Four molecules per homooctamer, crystallization data
Mn2+
-
required at different concentrations in the different subcellular fractions, overview
Mn2+
G7YVB4
stimulation increases in the order Mg2+, Mn2+, Zn2+, Cu2+. Mg2+ stimulates below 5 mM, inhibits above 10 mM
Mn2+
-
divalent cation required. Mn2+ or Mg2+; less active in activation than Mg2+
Mn2+
the omission of 2 mM Mn2+ in assay results in 90% loss of activity
Mn2+
divalent metal cations are required for enzymatic activity. However, only Mn2+ supports activity of GlpX and YggF; divalent metal cations are required for enzymatic activity. Mn2+ supports activity of GlpX and YggF
Mn2+
-
or Mg2+, required. Km-value for Mn2+ is 0.062 mM. Mn2+ enhances Mg2+ activated enzyme activity
Mn2+
-
divalent cation required. Mn2+ or Mg2+; optimal concentration at pH 7.5: 0.05-0.07 mM
Mn2+
-
divalent cation required. Mn2+ or Mg2+; Mn2+ is significantly more effective than Mg2+; optimal concentration: 0.05-0.075 mM
Mn2+
-
can substitute for Mg2+ with 50% efficiency, enzyme from methanol-grown cells
Mn2+
-
divalent cation required. Mn2+ or Mg2+; Km: 0.022 mM; Km: 0.078 mM
Mn2+
-
absolute requirement for divalent cation, fulfilled by Mg2+, Zn2+, Mn2+, both Zn2+ and Mn2+ are inhibitory above 3 mM
Zn2+
G7YVB4
stimulation increases in the order Mg2+, Mn2+, Zn2+, Cu2+. Mg2+ stimulates below 5 mM, inhibits above 10 mM
Zn2+
-
strong inhibitor at low concentrations, activator at high concentrations
Zn2+
-
absolute requirement for divalent cation, fulfilled by Mg2+, Zn2+, Mn2+, both Zn2+ and Mn2+ are inhibitory above 3 mM
additional information
-
no significant activation: Co2+, Ni2+, Cu2+, Zn2+, Fe2+, and Ca2+; no significant activation: Co2+, Ni2+, Cu2+, Zn2+, Fe2+, and Ca2+
additional information
no significant activation: Co2+, Ni2+, Cu2+, Zn2+, Fe2+, and Ca2+; no significant activation: Co2+, Ni2+, Cu2+, Zn2+, Fe2+, and Ca2+
additional information
Q6TV42
no significant activation: Co2+, Ni2+, Cu2+, Zn2+, Fe2+, and Ca2+; no significant activation: Co2+, Ni2+, Cu2+, Zn2+, Fe2+, and Ca2+
additional information
-
the enzyme activity is dependent on bivalent metal ions, but Co2+, Ni2+, Cu2+, Zn2+, Fe2+ and Ca2+ show no significant activation of FBPase at any specific concentration
additional information
the enzyme is independent of metals, Mg2+, Mn2+, Co2+, Ni2+, Li+, and Ca2+ show no effect on activity
additional information
-
monovalent cations activate by helping the Arg 276 residue 'deshield' the partial negative charge on the 1-phosphoryl group of the substrate so that nucleophilic attack on the 1-phosphorus atom is facilitated
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2,3-diethoxy-7,8,9,10-tetrahydro-6H-cyclohepta[b]quinolin-11-yl)[3-(2-methylthiazol-4-yl)phenyl]amine
-
-
(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
-
-
(2-aminomethyl-6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)[3-(2-methylthiazol-4-yl)phenyl]-amine
-
-
(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
(6,7-diethoxy-1,2,3,4-tetrahydroacridin-9-yl)[3-(2-methylthiazol-4-yl)phenyl]amine
-
-
(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)[3-(2-methylthiazol-4-yl)phenyl]amine
-
-
1-Fluoro-2,4-dinitrobenzene
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
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
2,5-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-(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-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl dihydrogen phosphate
-
-
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
3,4-dihydroxy-N'-[(E)-[4-oxo-6-(propan-2-yl)-4H-chromen-3-yl]methylidene]benzohydrazide
-
compound potently inhibits both fructose-1,6-bisphoshate aldolase and fructose-1,6-bisphosphatase with IC50 values below 30 microM
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-[[(2R,4S)-4-(3-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
4-[[(2R,4S)-4-(3-methoxyphenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
4-[[(2R,4S)-4-(4-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
4-[[(2S,4S)-4-(3-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
4-[[(2S,4S)-4-(3-methoxyphenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
4-[[(2S,4S)-4-(4-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
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
6,7-diethoxy-N-[3-(2-methyl-1,3-thiazol-4-yl)phenyl]quinazolin-4-amine
-
-
6,7-dimethyl-4-[[(2R,4S)-2-oxido-4-(pyridin-2-yl)-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
-
-
6,7-dimethyl-4-[[(2R,4S)-2-oxido-4-(pyridin-3-yl)-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
-
-
6,7-dimethyl-4-[[(2R,4S)-2-oxido-4-(pyridin-4-yl)-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
-
-
6,7-dimethyl-4-[[(2R,4S)-4-(2-methylpyridin-3-yl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
-
-
6,7-dimethyl-4-[[(2R,4S)-4-(6-methylpyridin-3-yl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
-
-
aminoimidazole carboxamide ribotide
-
inhibition of fructose-1,6-bisphosphatase by aminoimidazole carboxamide ribotide prevents growth of Salmonella enterica purH mutants on glycerol
ammonium sulfate
-
10 mM, 127% of initial activity, 50 mM, no residual activity
anilinoquinazoline
-
low molecular weight inhibitors of enzyme that are not substrate mimics or AMP analogues
-
D-fructose 6-phosphate
-
mixed-type. AMP, D-fructose 6-phosphate, D-fructose 1,6-bisphosphate interact in a synergistic way to inhibit the enzyme activity
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
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 (2S,6S)-4-[[(6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazol-4-yl)oxy]methyl]-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)
-
-
fructose 2,6-bisphosphate
-
global conformational change in porcine FBPase induced by fructose 2,6-bisphosphate in the absence of AMP
fructose-2,6-bisphosphate
50% inhibition in the presence of 0.2 mM fructose-1,6-bisphosphate
L-alanine, N,N'-[[5-[2-amino-5-(2-methylpropyl)-4-thiazolyl]-2-furanyl] phosphinylidene]bis-, diethyl ester
-
effect of gluconeogenesis inhibition on postprandial hyperglycemia is investigated using the inhibitor CS-917 in meal-loaded diabetic Goto-Kakizaki rats. CS-917 suppresses plasma glucose elevation after meal loading in a dose-dependent manner at doses ranging from 10 to 40 mg/kg. In an overnight-fasted state, CS-917 decreases the plasma glucose levels dose-dependently at doses ranging from 2.5 to 40 mg/kg. Glucose-lowering is associated with an accumulation of hepatic D-fructose 1,6-bisphosphate and a reduction in hepatic D-fructose 6-phosphate. Chronic treatment of CS-917 decreases plasma glucose significantly, and no significant increase in plasma lactate and no profound elevation in plasma triglycerides are observed by both acute and chronic treatment of CS-917 in Goto-Kakizaki rats
N'-[(E)-(6-ethyl-4-oxo-4H-chromen-3-yl)methylidene]-3,4-dihydroxybenzohydrazide
-
compound potently inhibits both fructose-1,6-bisphoshate aldolase and fructose-1,6-bisphosphatase with IC50 values below 30 microM
N'-[(E)-(6-tert-butyl-4-oxo-4H-chromen-3-yl)methylidene]-3,4-dihydroxybenzohydrazide
-
compound potently inhibits both fructose-1,6-bisphoshate aldolase and fructose-1,6-bisphosphatase with IC50 values below 30 microM
N,N'-bis(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)pentane-1,5-diamine
-
uncompetitive
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)butan-1,4-diamine
-
0.03 mM, 20% inhibition
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)hexan-1,6-diamine
-
-
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)pentan-1,5-diamine
-
-
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)propan-1,3-diamine
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfamide
-
excellent bioavailability and a good pharmacokinetic profile in rats
N-(6,7-diethoxy-9-[3-(2-methylthiazol-4-yl)phenylamino]-2,3-dihydro-1H-cyclopenta[b]quinolin-1-yl)-acetamide
-
-
N-(6,7-diethoxy-9-[3-(2-methylthiazol-4-yl)phenylamino]-2,3-dihydro-1H-cyclopenta[b]quinolin-2-yl)acetamide
-
-
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-[(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
NaCl
-
in vivo: The presence of 100 mM NaCl in the growth medium only marginally alters the cytosolic and chloroplastic enzyme activities of salt-tolerant varieties whereas both the activities decline appreciably in salt-sensitive varieties tested. in vitro: comparison of inhibition of chloroplastic enzyme in a salt-sensitive and a salt-tolerant enzyme, protection against inhibition in salt-sensitve rice by mannitol, inositol, pinitol, sorbitol, trehalose, sucrose and proline
NEM
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
p-mercuribenzoate
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
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
-
-
pseudo-tetrapeptide OC252
-
the inhibition is synergistic with both AMP and fructose 2,6-bisphosphate, noncompetitive with respect to Mg2+ and, uncompetitive with respect to fructose 1,6-bisphosphate
Ribulose 1,5-diphosphate
-
1 mM, 48% inhibition of isoenzyme A, 3% inhibition of isoenzyme B
sedoheptulose 1,7-diphosphate
-
competitive inhibition of activity with fructose 1,6-diphosphate
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
-
-
[(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)(difluoro)methyl]phosphonic acid
-
-
[(2R,3S,4R,5R)-5-[4-(aminocarbonyl)-1H-imidazol-1-yl]-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen phosphate
-
-
[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-(2-amino-5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
non-competitive
[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-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-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-6,7-dichloro-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-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-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-5-fluoro-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
[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
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
-
-
(5-[4-amino-7-[3-(dimethylamino)propyl]-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-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
-
-
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
50% inhibition at 0.0034 mM
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
non-competitive
2-amino-4-[2-(5-phosphono)furanyl]-5-ethoxycarbonylthiazole
-
potent FBPase inhibitor
2-amino-4-[2-(5-phosphono)furanyl]-5-ethoxycarbonylthiazole
-
potent FBPase inhibitor: when administerd intravenously it lowers plasma glucose levels in 18 h fasted normal Sprague-Dawley rats above 50% at doses below 10 mg/kg
2-amino-4-[2-(5-phosphono)furanyl]-5-isobutylthiazole
-
potent FBPase inhibitor: when administerd intravenously it lowers plasma glucose levels in 18 h fasted normal Sprague-Dawley rats above 50% at doses below 10 mg/kg
2-amino-4-[2-(5-phosphono)furanyl]-5-phenylthiazole
-
potent FBPase inhibitor: when administerd intravenously it lowers plasma glucose levels in 18 h fasted normal Sprague-Dawley rats above 50% at doses below 10 mg/kg
2-amino-4-[2-(5-phosphono)furanyl]-5-propylsulfanylthiazole
-
potent FBPase inhibitor
2-amino-4-[2-(5-phosphono)furanyl]-5-propylsulfanylthiazole
-
potent FBPase inhibitor: when administerd intravenously it lowers plasma glucose levels in 18 h fasted normal Sprague-Dawley rats above 50% at doses below 10 mg/kg
2-amino-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
poor oral bioavailability
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-methylsulfanyl-4-[2-(5-diethylphosphono)furanyl]thiazole
-
potent FBPase inhibitor: when administerd intravenously it lowers plasma glucose levels in 18 h fasted normal Sprague-Dawley rats above 50% at doses below 10 mg/kg
2-[3-methyl-5-([[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)thiophen-2-yl]ethyl acetate
-
-
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
-
-
2-[5-([[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)-3-methylthiophen-2-yl]ethyl acetate
-
-
5-(2-hydroxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
-
-
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-([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-[[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)-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
-
-
5-(2-methoxyethyl)-N-([4-methoxy-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-4-methylthiophene-2-sulfonamide
-
-
AMP
-
transformation of enzyme to inactive T-state, inhibition shows quarternary transition and cooperativity
AMP
-
FBPase undergoes a quaternary transition from the canonical R-state to a T-like state in response to AMP. Glc-6-P and AMP are synergistic inhibitors
AMP
-
AMP and D-fructose 2,6-bisphosphate are not synergistic inhibitors of the type I FBPase
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
AMP
-
113Tyr and 31Thr play an mportant role, each via two hydrogen bonds affecting the binding affinity of inhibitor AMP to FBPase
AMP
-
non-competitive. AMP, D-fructose 6-phosphate, D-fructose 1,6-bisphosphate interact in a synergistic way to inhibit the enzyme activity
AMP
-
sensitivity decreases greatly with increasing pH or temperature. Inhibition of Zn2+ and AMP is synergistic
AMP
-
sensitivity to AMP is decreased with increase in pH, temperature and Mg2+ concentration
AMP
-
-
AMP
-
non-competitive inhibition of cytosolic enzyme, the chloroplastic enzyme is AMP-insensitive
AMP
-
non-competitive inhibition of cytosolic enzyme, the chloroplatic enzyme is AMP-insensitive
AMP
-
acts synergistically with fructose-2,6-bisphosphate on the frog muscle FBPase
AMP
-
muscle enzyme: 50% inhibition at 0.00054 mM, liver enzyme: 50% inhibition at 0.085 mM
AMP
-
0.1 mM, 9% inhibition of isoenzyme A, complete inhibition of isoenzyme B
AMP
-
the phosphoenzyme is about 3fold more sensitive than the dephosphoenzyme
AMP
-
uptake of 1 M of NEM per mol of subunit is accompanied by a loss of sensitivity towards AMP. K+ induces a conformational change on the enzyme derivative which hinders AMP interaction with the protein
AMP
-
study of allosteric inhibition, two classes of binding sites with two distinct affinities for AMP are possible
AMP
-
wild-type, 50% inhibition at 0.0016 mM, mutant E97A, 50% inhibition at 0.0038 mM, mutant D118A, 50% inhibition at 0.0069 mM, mutant D121A, 50% inhibition at 0.0074 mM
AMP