HOME
login
history
all enzymes
BRENDA home
History
Information on EC 3.1.3.11 - fructose-bisphosphatase
for references in articles please use BRENDA:EC3.1.3.11Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.1.3.11 fructose-bisphosphataseIUBMB Comments
The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
Specify your search results
Word Map
- 3.1.3.11
- fbpases
-
gluconeogenesis
-
gluconeogenic
- amp
- chloroplast
- phosphoenolpyruvate
-
carboxykinase
- glycogen
- glucose-6-phosphatase
- diabetes
- insulin
-
phosphofructokinase
- 2,6-bisphosphate
- hexokinase
- spinach
- thioredoxins
- malate
- carboxylase
- starch
- phosphorylase
- fructose-2,6-bisphosphate
- glucokinase
- pepck
-
6-phosphatase
-
amp-dependent
- 3-phosphoglycerate
-
calvin
- dihydroxyacetone
- glucagon
- oleracea
- triose
- ribulose-1,5-bisphosphate
- fructose-6-phosphate
- g6pase
-
nadp-malate
- sedoheptulose
-
sucrose-phosphate
-
light-activated
-
triose-phosphate
- 6-phosphofructo-1-kinase
-
antihyperglycemic
- rubisco
- trx
- phosphoribulokinase
- ribulose
-
calvin-benson
- molecular biology
-
monophosphatase
-
t-states
- synthesis
- diagnostics
- medicine
- rubp
-
2.7.1.11
- drug development
- biotechnology
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
AF2372, archaeal FBP aldolase/phosphatase, archaeal-like fructose-1,6-bisphosphatase, beta-PGM, BiBPase, bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase, bifunctional fructose-1,6-bisphosphate aldolase/phosphatase, cFBP1, CFBPase, class II FBPase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
archaeal FBP aldolase/phosphatase
archaeal-like fructose-1,6-bisphosphatase
beta-PGM
BiBPase
bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase
-
bifunctional fructose-1,6-bisphosphate aldolase/phosphatase
-
CFBPase
class II FBPase
class II fructose-1,6-bisphosphatase
CpFBP1
CY-F1
-
-
-
-
cyanobacterial fructose-1,6-bisphosphatase
cyanoFBPase-II
cytosolic FBPase
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
-
-
-
-
dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase
-
EgFBPaseI
EgFBPaseII
EgFBPaseIII
F16BDEPHOS
Fbp
FBP aldolase/phosphatase
FBP-1
FBP1
FBPase
FBPase II
FBPase IV
the enzyme is present in euryarchaeal and hyperthermophilic bacterial species
FBPase-1
FBPaseII
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-bisphosphatase-1
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
-
-
-
-
ImpA
IMPase A
MtFBPaseII
MtFPBase
neutral FBPase
RAE-30
-
-
-
-
slr2094
STK_03180
locus name. The bifunctional enzyme also shows activity of EC 4.1.2.13
SYNPCC7002_A1301
additional information
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
additional information
YK23 is a member of the histidine phosphatase (phosphoglyceromutase) superfamily
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
the proposed mechanism involves two metal ions near the cleavable phosphate: one to stabilize the negative charge on the leaving group and one to coordinate the nucleophilic water
-
D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
metal-dependent reaction mechanism, allosteric mechanism of the enzyme, overview
D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
the proposed mechanism involves two metal ions near the cleavable phosphate: one to stabilize the negative charge on the leaving group and one to coordinate the nucleophilic water
-
-
D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
KEGG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
D-fructose-1,6-bisphosphate 1-phosphohydrolase
The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9001-52-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
5-phospho-D-ribosyl diphosphate + H2O
?
40.73% activity compared to D-fructose 1,6-bisphosphate
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
Kluyveromyces marxianus UFS-2791
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
preferred substrate
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
Synechococcus sp. PCC 7002 ATCC 27264
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Synechococcus sp. PCC 7002 PR-6
-
-
-
?
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
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
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
Mycolicibacterium smegmatis ATCC 700084
-
-
-
?
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
?
-
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
?
-
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
?
-
-
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
?
-
-
bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
-
-
-
additional information
?
-
-
the higher Km for D-fructose 1,6-bisphosphate of LmFBPase compared to the Escherichia coli enzyme may be explained by a sequence difference at the active site, with Tyr221 replaced by Asn221 resulting in the loss of a direct hydrogen bond with substrate D-fructose 1,6-bisphosphate. Binding structure analysis of substrate and product, overview
-
-
-
additional information
?
-
the higher Km for D-fructose 1,6-bisphosphate of LmFBPase compared to the Escherichia coli enzyme may be explained by a sequence difference at the active site, with Tyr221 replaced by Asn221 resulting in the loss of a direct hydrogen bond with substrate D-fructose 1,6-bisphosphate. Binding structure analysis of substrate and product, overview
-
-
-
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
?
-
-
substrate binding analysis of wild-type and mutant enzymes by surface plasmon resonance method, substrate affinities, overview
-
-
-
additional information
?
-
-
substrate binding analysis of wild-type and mutant enzymes by surface plasmon resonance method, substrate affinities, overview
-
-
-
additional information
?
-
substrate binding analysis of wild-type and mutant enzymes by surface plasmon resonance method, substrate affinities, overview
-
-
-
additional information
?
-
purified recombinant Pcal_0111 catalyzes both phosphatase and aldolase reactions with specific activity values of 4 U and 1.3 U, respectively. Although the enzyme can utilize several substrates for dephosphorylation, no phosphatase activity is detected with AMP, UTP, NADP, glucose 6-phosphate, ribose 5-phosphate, riboflavin 5-monophosphate, and pyridoxal 5-phosphate. Varying amounts of phosphatase activity are found when ATP, GTP, ADP, CTP, glyceraldehyde 3-phosphate, fructose 6-phosphate, fructose 1,6-bisphosphate, and phosphoribosyl diphosphate are used as substrates. The highest phosphatase activity is found with fructose 1,6-bisphosphate followed by phosphoribosyl diphosphate. Spectrophotometric coupled enzyme assay as discontinuous assay method, or product phosphate detection by malachite green assay method. Substrate binding residues include Tyr229, Lys232, and Tyr358
-
-
-
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
-
-
-
additional information
?
-
a dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase (FBP/SBPase) exhibiting activity of EC 3.1.3.37, sedoheptulose 1,7-diphosphatase, and 3.1.3.11, fructose 1,6-bisphosphatase
-
-
-
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
A8IKQ0
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
A8IKQ0
-
-
-
?
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
A0A0U4MTX7
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
A0A0U5BQA3, A3QSS7
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
A0A0U4MTX7
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
A0A0U5BQA3, A3QSS7
-
-
-
?
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
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
O00757
-
-
-
?
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
Kluyveromyces marxianus UFS-2791
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
O97193
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
P9WN21
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
P9WN21
-
-
-
?
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
P9WN21
-
-
-
?
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
P46275
-
-
-
?
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
A3MSD2
-
-
-
?
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
P19112
-
-
-
?
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
P19112
-
-
-
?
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
T1W0T2
-
-
-
?
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
B1XLK5
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Synechococcus sp. PCC 7002 ATCC 27264
B1XLK5
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Synechococcus sp. PCC 7002 PR-6
B1XLK5
-
-
-
?
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
Q8DJE9
-
-
-
?
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
-
-
-
additional information
?
-
Q8DJE9
a dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase (FBP/SBPase) exhibiting activity of EC 3.1.3.37, sedoheptulose 1,7-diphosphatase, and 3.1.3.11, fructose 1,6-bisphosphatase
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
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
Mg2+
-
activates, required for activity, Ka values for wild-type and mutant enzymes, kinetics, overview
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
no significant activation: Co2+, Ni2+, Cu2+, Zn2+, Fe2+, and Ca2+; no significant activation: Co2+, Ni2+, Cu2+, Zn2+, Fe2+, and Ca2+
additional information
metal binding structure of the enzyme, overview
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 apoenzyme does not contain Mg2+ in the active site, instead Mg2+ is found in helices H8 and H9 in one chain, coordinated to Leu165 N, Gln164 N and Arg161 O and possibly stabilizing this loop. The fructose 6-phosphate-bound structures contain one magnesium ion in a position that is proposed to bind fructose 1,6-bisphosphate, coordinate the 1-phosphate and stabilize the transition state
additional information
residues involved in metal binding include Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357
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-(cyclopropyl)methyl-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
-
-
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-(2-carboxyethyl)-7-nitro-4-(3-methoxyphenylamino)-1H-indole-2-carboxylic acid
-
-
3-(2-carboxyethyl)-7-nitro-4-(4-methoxyphenylamino)-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-[[(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 2,6-bisphosphate