Information on EC 4.1.2.13 - fructose-bisphosphate aldolase

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

EC NUMBER
COMMENTARY
4.1.2.13
-
RECOMMENDED NAME
GeneOntology No.
fructose-bisphosphate aldolase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
in class I fructose diphosphate aldolases a Schiff base intermediate is formed between glycerone phosphate or fructose 1,6-diphosphate and an epsilon-amino group of a Lys residue at the active site of the enzyme
-
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
in class I fructose diphosphate aldolases a Schiff base intermediate is formed between glycerone phosphate or fructose 1,6-diphosphate and an epsilon-amino group of a Lys residue at the active site of the enzyme
-
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
in class I fructose diphosphate aldolases a Schiff base intermediate is formed between glycerone phosphate or fructose 1,6-diphosphate and an epsilon-amino group of a Lys residue at the active site of the enzyme
-
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
proton-transfer mechanism involving Lys-229, Glu-187 and Lys-146
-
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
mechanism and energetic aspects of class I aldolases
-
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
ordered uni-bi reaction mechanism
-
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
the enzyme binds and utilizes only the carbonyl forms of fructose 1,6-diphosphate and glycerone phosphate
-
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Schiff base intermediate is formed at the epsilon-amino group of Lys229
-
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
mechanism
-
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
mechanism of class II aldolase
-
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
mechanism
-
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
fructose-1,6-bisphosphate aldolase cytosolic class I as an NMH7 MADS domain-associated protein
-
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
in class I fructose diphosphate aldolases a Schiff base intermediate is formed between glycerone phosphate or fructose 1,6-diphosphate and an epsilon-amino group of a Lys residue at the active site of the enzyme
Peptoniphilus asaccharolyticus 228
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
-
-
-
-
elimination
-
-
of an aldehyde, C-C bond cleavage
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,3-propanediol biosynthesis (engineered)
-
-
Calvin-Benson-Bassham cycle
-
-
formaldehyde assimilation II (RuMP Cycle)
-
-
formaldehyde assimilation III (dihydroxyacetone cycle)
-
-
gluconeogenesis I
-
-
gluconeogenesis II (Methanobacterium thermoautotrophicum)
-
-
gluconeogenesis III
-
-
glycolysis I (from glucose 6-phosphate)
-
-
glycolysis II (from fructose 6-phosphate)
-
-
glycolysis III (from glucose)
-
-
glycolysis IV (plant cytosol)
-
-
glycolysis V (Pyrococcus)
-
-
glycolysis VI (metazoan)
-
-
sucrose biosynthesis I (from photosynthesis)
-
-
sucrose degradation V (sucrose alpha-glucosidase)
-
-
glycolysis
-
-
photosynthesis
-
-
Glycolysis / Gluconeogenesis
-
-
Pentose phosphate pathway
-
-
Fructose and mannose metabolism
-
-
Methane metabolism
-
-
Carbon fixation in photosynthetic organisms
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Microbial metabolism in diverse environments
-
-
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase (glycerone-phosphate-forming)
Also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1,6-Diphosphofructose aldolase
-
-
-
-
37 kDa major allergen
-
-
-
-
41 kDa antigen
-
-
-
-
aldoA
-
-
aldoA
-
-
aldolase
-
-
-
-
aldolase A
-
-
aldolase A
-
-
aldolase B
-
-
aldolase B
-
-
aldolase C
-
-
aldolase C
-
brain-specific isoform of fructose bisphosphate aldolase
aldolase, fructose diphosphate
-
-
-
-
ALDP
-
-
-
-
Brain-type aldolase
-
-
-
-
CE1
-
-
-
-
CE2
-
-
-
-
class I Fba
-
-
class I fructose 1,6-bisphosphate aldolase
-
-
class I fructose bisphosphate aldolase
-
class I muscle fructose bis-phosphate aldolase
-
class II aldolase
-
class II aldolase
-
class II FBP aldolase
-
class II FBP aldolase
-
-
class II fructose 1,6-bisphosphate aldolase
-
-
class II fructose 1,6-bisphosphate aldolase
-
-
-
class II fructose 1,6-bisphosphate aldolase
-
-
class II fructose bisphosphate aldolase
-
class II fructose bisphosphate aldolase
-
class II fructose bisphosphate aldolase
-
-
class II fructose bisphosphate aldolase
-
class II fructose-1,6-bisphosphate aldolase
-
-
class II fructose-1,6-bisphosphate aldolase
Haloferax mediterranei DSM 1411
-
-
-
class II fructose-1,6-bisphosphate aldolase
-
class II fructose-1,6-bisphosphate aldolase
-
-
class IIa fructose 1,6-bisphosphate aldolase
-
class IIa fructose 1,6-bisphosphate aldolase
-
-
ClassII FBP-aldolase
-
-
D-fructose-1,6-bisphosphate aldolase
-
-
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-P-lyase
-
-
Diphosphofructose aldolase
-
-
-
-
DLF
-
bifunctional enzyme, consists of monomeric fructose-1,6-bisphosphate aldolase from Staphylococcus carnosus and the homodimeric dihydroxyacetone kinase from Citrobacter freundii CECT 4626 with an intervening linker of five amino acid residues
DLF
Staphylococcus carnosus CECT 4491
-
bifunctional enzyme, consists of monomeric fructose-1,6-bisphosphate aldolase from Staphylococcus carnosus and the homodimeric dihydroxyacetone kinase from Citrobacter freundii CECT 4626 with an intervening linker of five amino acid residues
-
EC 4.1.2.7
-
-
formerly
-
F1,6P2 aldolase
-
-
FBA
Haloferax volcanii DSM 3757
-
-
FBA
the Methylococcus capsulatus enzyme belongs to the type B of class II fructose-1,6-bisphosphate aldolases
FBP aldolase
-
-
-
-
FBP aldolase
Anoxybacillus gonensis G2
-
-
FBP aldolase
-
-
FBP aldolase
-
-
-
FBP aldolase
-
-
FBP aldolase
-
-
FBP aldolase
Haloferax mediterranei DSM 1411
-
-
-
FBP aldolase
-
-
FBP aldolase
-
-
FBP aldolase
-
-
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
Pyrobaculum neutrophilum DSM 2338
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
Sulfolobus tokodaii 7
bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13
-
FBPA
Schistosoma japonicum Formosan
-
-
FBPA
Staphylococcus carnosus CECT 4491
-
-
-
FBPA/P
bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13
FBPA/P
Sulfolobus tokodaii 7
bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13
-
FDP aldolase
-
-
FPA
-
-
Fru-1,6-P2 aldolase
-
-
Fru-P2A
-
-
-
-
Fructoaldolase
-
-
-
-
fructose 1,6 bisphosphate aldolase
-
Fructose 1,6-bisphosphate aldolase
-
-
-
-
Fructose 1,6-bisphosphate aldolase
-
-
Fructose 1,6-bisphosphate aldolase
-
-
Fructose 1,6-bisphosphate aldolase
-
fructose 1,6-bisphosphate aldolase/phosphatase
-
bifunctional enzyme with both fructose 1,6-bisphosphate aldolase and fructose 1,6-bisphosphate phosphatase activity
Fructose 1,6-diphosphate aldolase
-
-
-
-
Fructose 1-monophosphate aldolase
-
-
-
-
Fructose 1-phosphate aldolase
-
-
-
-
fructose bis-phosphate aldolase
-
fructose bis-phosphate aldolase
-
fructose bis-phosphate aldolase
-
Fructose bisphosphate aldolase
-
-
-
-
Fructose bisphosphate aldolase
-
-
Fructose bisphosphate aldolase
-
Fructose bisphosphate aldolase
-
-
Fructose bisphosphate aldolase
-
Fructose bisphosphate aldolase
-
-
Fructose bisphosphate aldolase
-
Fructose diphosphate aldolase
-
-
-
-
fructose-1,6-biphosphate aldolase
-
-
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 (FBP) aldolase/phosphatase
Pyrobaculum neutrophilum DSM 2338
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
-
fructose-1,6-bisphosphate aldolase
-
-
fructose-1,6-bisphosphate aldolase
-
fructose-1,6-bisphosphate aldolase
Haloferax volcanii DSM 3757
-
-
fructose-1,6-bisphosphate aldolase
-
-
fructose-1,6-bisphosphate aldolase
-
-
fructose-1,6-bisphosphate aldolase
-
fructose-1,6-bisphosphate aldolase
-
-
fructose-1,6-bisphosphate aldolase
-
fructose-1,6-bisphosphate aldolase
-
fructose-1,6-bisphosphate aldolase
Schistosoma japonicum Formosan
-
-
fructose-1,6-bisphosphate aldolase
-
-
fructose-1,6-bisphosphate aldolase
-
-
fructose-1,6-bisphosphate aldolase
Staphylococcus carnosus CECT 4491
-
-
-
fructose-1,6-bisphosphate aldolase
-
-
fructose-1,6-bisphosphate aldolase A
-
-
fructose-1,6-bisphosphate aldolase A
-
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
Pyrobaculum neutrophilum DSM 2338
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
fructose-1,6-bisphosphate aldolase/phosphatase
Sulfolobus tokodaii 7
bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13
-
fructose-1,6-bisphosphate muscle aldolase
-
-
Fructose-1,6-bisphosphate triosephosphate-lyase
-
-
-
-
fuculose aldolase
-
-
heat-induced protein 44
-
-
HIP44
-
-
IgE-binding allergen
-
-
-
-
ketose 1-phosphate aldolase
-
-
-
-
Leishmania aldolase
-
-
Leishmania aldolase
Leishmania donovani 2S
-
-
-
Liver-type aldolase
-
-
-
-
MGA3_01355
gene name
MGA3_01355
gene name
-
Muscle-type aldolase
-
-
-
-
Phosphofructoaldolase
-
-
-
-
SMALDO
-
-
-
-
SSO0286
locus name
-
STK_03180
locus name. The bifunctional enzyme also shows activity of EC 3.1.3.11
STK_03180
Sulfolobus tokodaii 7
locus name. The bifunctional enzyme also shows activity of EC 3.1.3.11
-
Tneu_0133
locus name
Tneu_0133
Pyrobaculum neutrophilum DSM 2338
locus name
-
TnFBPAP
Pyrobaculum neutrophilum DSM 2338
-
-
zymohexase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-52-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Anacystis sp.
-
-
-
Manually annotated by BRENDA team
Anoxybacillus gonensis G2
strain G2
EMBL
Manually annotated by BRENDA team
Archaeoglobus fulgidus 7324
-
-
-
Manually annotated by BRENDA team
strain NRRL 3435, strain NRRL 447, strain NRRL 480 and strain NRRL 3484
-
-
Manually annotated by BRENDA team
cv. Victory 1, oat
-
-
Manually annotated by BRENDA team
strain ATCC 19213
-
-
Manually annotated by BRENDA team
chromosomally located isoform FbaC
UniProt
Manually annotated by BRENDA team
chromosomally located isoform FbaC
UniProt
Manually annotated by BRENDA team
strain PCI 219 and strain 168
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
golden-mantled ground squirrel
-
-
Manually annotated by BRENDA team
Candida sp.
-
-
-
Manually annotated by BRENDA team
Chlamydomonas sp.
-
-
-
Manually annotated by BRENDA team
Crookes' strain
-
-
Manually annotated by BRENDA team
Escherichia coli Crookes
Crookes' strain
-
-
Manually annotated by BRENDA team
Euglena sp.
-
-
-
Manually annotated by BRENDA team
domesticus
-
-
Manually annotated by BRENDA team
Haloferax mediterranei DSM 1411
-
-
-
Manually annotated by BRENDA team
Haloferax volcanii DSM 3757
-
SwissProt
Manually annotated by BRENDA team
patients with fructose intolerance
-
-
Manually annotated by BRENDA team
strain 2S
-
-
Manually annotated by BRENDA team
Leishmania donovani 2S
strain 2S
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
C3KO or wild-type mice
-
-
Manually annotated by BRENDA team
CDC No. 46
-
-
Manually annotated by BRENDA team
H37Rv, NCTC, 7416: aldolase class I; NCTC, 7416: aldolase class II
-
-
Manually annotated by BRENDA team
L. cv. Nipponbare
-
-
Manually annotated by BRENDA team
Peptoniphilus asaccharolyticus 228
strain 228
-
-
Manually annotated by BRENDA team
L. var. Littel Marvel
-
-
Manually annotated by BRENDA team
i.e. Thermoproteus neutrophilus
UniProt
Manually annotated by BRENDA team
Pyrobaculum neutrophilum DSM 2338
i.e. Thermoproteus neutrophilus
UniProt
Manually annotated by BRENDA team
adult worm
UniProt
Manually annotated by BRENDA team
Formosan strain
UniProt
Manually annotated by BRENDA team
Schistosoma japonicum Formosan
Formosan strain
UniProt
Manually annotated by BRENDA team
ATCC 12600
-
-
Manually annotated by BRENDA team
Staphylococcus carnosus CECT 4491
-
-
-
Manually annotated by BRENDA team
Sulfolobus tokodaii 7
-
UniProt
Manually annotated by BRENDA team
PCC 6803
-
-
Manually annotated by BRENDA team
exhibits light-activated heterotrophic growth (LAHG) under dark conditions with glucose as a carbon source
UniProt
Manually annotated by BRENDA team
strain GK24
Uniprot
Manually annotated by BRENDA team
Thermus caldophilus GK24
strain GK24
Uniprot
Manually annotated by BRENDA team
Veillonella sp.
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
deletion mutant loses the ability to grow on fructose, but growth on glucose is not inhibited and is even slightly stimulated
malfunction
Haloferax volcanii DSM 3757
-
deletion mutant loses the ability to grow on fructose, but growth on glucose is not inhibited and is even slightly stimulated
-
metabolism
-
chloroplastic fructose 1,6-bisphosphate aldolase isoforms are methylated by protein-lysine methyltransferase LSMT. Trimethylation occurs at a conserved lysyl residue located close to the C terminus. Trimethylation does not modify the kinetic properties and tetrameric organization of the aldolases in vitro
physiological function
-
part of 4-fluorothreonine biosynthesis
physiological function
-
ALDOA is involved in keratinocyte migration following the induction of lamellipodia formation, and ALDOA-related migration is enhanced by epidermal growth factor
physiological function
-
FBA is required for optimal adhesion of meningococci to human cells
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis. The enzyme is essential for growth on fructose
physiological function
gluconeogenic pathway
physiological function
-
the overproduction of fructose bisphosphate aldolase Fba1 enables overcoming of a severe growth defect caused by a missense mutation rpc128-1007 in a gene encoding the C128 protein, the second largest subunit of the RNA polymerase III complex. The suppression of the growth phenotype by Fba1 is accompanied by enhanced de novo tRNA transcription in rpc128-1007 cells. Overproduction of an inactive aldolase mutant still suppresses the rpc128-1007 phenotype, and Fba1 interacts with the RNA polymerase III complex and plays a role in control of tRNA transcription
physiological function
-
the enzyme is involved in glycogen catabolism
physiological function
-
gene product is required for the growth of Mycobacterium tuberculosis on gluconeogenetic substrates and in glucose-containing medium
physiological function
-
transgenic Nicotiana tabacum L. cv Xanthi expressing Arabidopsis plastid aldolase shows 1.4-1.9fold higher aldolase activities than wild-type, associated with enhanced growth, culminating in increased biomass, particularly under high CO2 concentration where the increase reached 2.2fold relative to wild-type plants. This increase is associated with a 1.5fold elevation of photosynthetic CO2 fixation in the transgenic plants. Overexpression results in a decrease in 3-phosphoglycerate and an increase in ribulose 1,5-bisphosphate and its immediate precursors in the Calvin cycle
physiological function
-
the seed germination and root elongation of knock-out plants exhibits sensitivity to abscisic acid and salt stress. Gene is able to complement the salt-sensitive phenotype of a calcineurin-deficient yeast mutant
physiological function
isoform FbaC acts as major aldolase in glycolysis, whereas isoform FbaP acts as major aldolase in gluconeogenesis in Bacillus methanolicus. The aldolase-negative Corynebacterium glutamicum mutant Dfda can be complemented by the FbaC gene; isoform FbaC acts as major aldolase in glycolysis, whereas isoform FbaP acts as major aldolase in gluconeogenesis in Bacillus methanolicus. The aldolase-negative Corynebacterium glutamicum mutant Dfda can be complemented by the FbaC gene
physiological function
-
mutagenesis in a unique fbaB gene of Xanthomonas oryzae pv. oryzicola, the causal agent of rice bacterial leaf streak, leads the pathogen unable to use pyruvate and malate for growth and delays its growth when fructose is used as the sole carbon source, but also reduces extracellular polysaccharide production and impairs bacterial virulence and growth in rice. The expression of hrpG and hrpX encoding a type-III secretion system is repressed and the transcripts of hrcC, hrpE and hpa3 are enhanced when fbaB is deleted
physiological function
Archaeoglobus fulgidus 7324
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
physiological function
-
isoform FbaC acts as major aldolase in glycolysis, whereas isoform FbaP acts as major aldolase in gluconeogenesis in Bacillus methanolicus. The aldolase-negative Corynebacterium glutamicum mutant Dfda can be complemented by the FbaC gene; isoform FbaC acts as major aldolase in glycolysis, whereas isoform FbaP acts as major aldolase in gluconeogenesis in Bacillus methanolicus. The aldolase-negative Corynebacterium glutamicum mutant Dfda can be complemented by the FbaC gene
-
physiological function
Haloferax volcanii DSM 3757
-
the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis. The enzyme is essential for growth on fructose
-
physiological function
-
gluconeogenic pathway
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 acetaldehyde
5-deoxy-D-threo-2-pentulose
show the reaction diagram
-
-
yield 29%
?
2 acetaldehyde
5-deoxy-D-threo-2-pentulose
show the reaction diagram
-
-
yield 33%
?
2 butyraldehyde
5,6,7-trideoxy-D-threo-2-heptulose
show the reaction diagram
-
-
yield 38%
?
2 butyraldehyde
5,6,7-trideoxy-D-threo-2-heptulose
show the reaction diagram
-
-
yield 40%
?
2 D-glyceraldehyde
D-fructose
show the reaction diagram
-
-
yield 60%
?
2 pentanaldehyde
5,6,7,8-tetradeoxy-D-threo-2-octulose
show the reaction diagram
-
-
yield 13%
?
2 pentanaldehyde
5,6,7,8-tetradeoxy-D-threo-2-octulose
show the reaction diagram
-
-
yield 23%
?
2 propionaldehyde
5,6-dideoxy-D-threo-2-hexulose
show the reaction diagram
-
-
yield 34%
?
2 propionaldehyde
5,6-dideoxy-D-threo-2-hexulose
show the reaction diagram
-
-
yield 37%
?
5-fluoro-5-deoxy-D-ribulose 1-phosphate
fluoroacetaldehyde + dihydroxyacetone phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
ir
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Lactobacillus sp., Chlamydomonas sp.
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Brucella sp., Erwinia sp., Veillonella sp., Saccharomyces sp., Candida sp., Aspergillus sp., Penicillium sp., Anacystis sp., Euglena sp.
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
high stereoselectivity for both newly created asymmetric centers
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
preferred substrate, reaction intermediate is Schiff base
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
preferred substrate, reaction intermediate is Schiff base
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
rate of reaction to form the Schiff-base intermediate is faster than ring-opening in solution
-
ir
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
enzyme uses a Schiff-base mechanism
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Peptoniphilus asaccharolyticus 228
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Leishmania donovani 2S
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Staphylococcus carnosus CECT 4491
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Archaeoglobus fulgidus 7324
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Anoxybacillus gonensis G2
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Haloferax volcanii DSM 3757
the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Haloferax mediterranei DSM 1411
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Escherichia coli Crookes
-
-
-
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Escherichia coli Crookes
-
-
-
-
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde 3-phosphate
show the reaction diagram
-
aldolase is involved in the metabolism of fructose, converting fructose 1-phosphate to dihydroxyacetone phosphate and glyceraldehyde
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
r
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
no activity
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
at 25% of the activity with fructose 1,6-diphosphate
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
muscle-type enzyme: at 3% of the activity with fructose 1,6-diphosphate
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
at 2% of the activity with fructose 1,6-diphosphate
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
at 3.5% of the activity with fructose 1,6-diphosphate
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
non-muscle-type enzyme: at about 23% of the activity with fructose 1,6-diphosphate
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
recombinant enzyme: 7.4% of the activity with fructose 1,6-diphosphate
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
at 15% of the activity with fructose 1,6-diphosphate
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
99% of the activity with fructose 1,6-diphosphate
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
5% of the activity with fructose 1,6-diphosphate
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
at 2.5% of the activity with fructose 1,6-diphosphate
-
-
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
the D-fructose 1,6-bisphosphate/D-fructose 1-phosphate cleavage ratio is 55:1
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
Peptoniphilus asaccharolyticus 228
-
-
-
-
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
-
-
-
?
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
-
-
-
?
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
-
-
r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
-
-
-
r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
-
-
-
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
-
-
-
r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
-
-
r
D-fructose-1,6-bisphosphate
glyceraldehyde-3-phosphate + dihydroxyacetone phosphate
show the reaction diagram
-
-
-
r
D-glyceraldehyde 3-phosphate + glycerone phosphate
tagatose-1,6-bisphosphate
show the reaction diagram
-
-
?
D-Xylulose 1-phosphate
?
show the reaction diagram
-
110% of the activity with fructose 1,6-diphosphate
-
-
-
dihydroxyacetone + phenyl [(2R)-1-oxopropan-2-yl]carbamate
phenyl [(2R,3R,4S)-3,4,6-trihydroxy-5-oxohexan-2-yl]carbamate
show the reaction diagram
-
i.e. (S)-N-Cbz-alaninal,substrate only for mutant A129S/A165G
aldol adduct is a key intermediates for the expedient synthesis of the pyrrolidine type iminocyclitol, 2,5-imino-1,2,5-trideoxy-D-mannitol
?
dihydroxyacetone + phenyl [(2S)-1-oxopropan-2-yl]carbamate
phenyl [(2S,3R,4S)-3,4,6-trihydroxy-5-oxohexan-2-yl]carbamate
show the reaction diagram
-
i.e. (S)-N-Cbz-alaninal, substrate only for mutant A129S/A165G
aldol adduct is a key intermediates for the expedient synthesis of the pyrrolidine type iminocyclitol, 2,5-imino-1,2,5-trideoxy-D-glucitol
?
dihydroxyacetone phosphate
?
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate
?
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
r
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
r
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
r
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
r
Glycerone phosphate + D-glyceraldehyde
Fructose 1-phosphate
show the reaction diagram
-
-
-
-
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
r
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
-
-
r
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
Brucella sp., Erwinia sp., Veillonella sp., Saccharomyces sp., Candida sp., Aspergillus sp., Penicillium sp., Anacystis sp., Euglena sp.
-
-
-
-
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
-
aldol synthesizing activity is only 1.5% of fructose 1,6-diphosphate cleavage
-
-
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
the bifunctional enzyme also shows activity of EC 3.1.3.11. 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
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
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, 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
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
-
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
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
Sulfolobus tokodaii 7
the bifunctional enzyme also shows activity of EC 3.1.3.11. 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
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
Pyrobaculum neutrophilum DSM 2338
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, 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
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
-
-
r
hydroxyacetone + phenoxyacetaldehyde
?
show the reaction diagram
-
substrate only for mutant A129S/A165G
-
-
?
hydroxyacetone + phenyl (2-oxoethyl)carbamate
?
show the reaction diagram
-
substrate only for mutant A129S/A165G
-
-
?
hydroxyacetone + phenyl (3-oxopropyl)carbamate
?
show the reaction diagram
-
substrate only for mutant A129S/A165G
-
-
?
hydroxyacetone + phenyl [(2R)-1-oxopropan-2-yl]carbamate
phenyl [(2R,3R,4S)-3,4-dihydroxy-5-oxohexan-2-yl]carbamate
show the reaction diagram
-
substrate only for mutant A129S/A165G
-
?
hydroxyacetone + phenyl [(2S)-1-oxopropan-2-yl]carbamate
phenyl [(2S,3R,4S)-3,4-dihydroxy-5-oxohexan-2-yl]carbamate
show the reaction diagram
-
substrate only for mutant A129S/A165G
-
?
propanal + dihydroxyacetone phosphate
?
show the reaction diagram
-
-
-
-
?
sedoheptulose 1,7-bis-phosphate
?
show the reaction diagram
-
-
-
-
?
sedoheptulose 1,7-bis-phosphate
glycerone phosphate + D-erythrose 4-phosphate
show the reaction diagram
-
-
-
?
sedoheptulose 1,7-bisphosphate
glycerone phosphate + D-erythrose 4-phosphate
show the reaction diagram
-
-
-
-
sedoheptulose 1,7-bisphosphate
glycerone phosphate + D-erythrose 4-phosphate
show the reaction diagram
-
-
-
?
sedoheptulose 1,7-bisphosphate
glycerone phosphate + D-erythrose 4-phosphate
show the reaction diagram
-
-
-
-
sedoheptulose 1,7-bisphosphate
glycerone phosphate + D-erythrose 4-phosphate
show the reaction diagram
-
-
?
sedoheptulose 1,7-bisphosphate
glycerone phosphate + D-erythrose 4-phosphate
show the reaction diagram
-
at 59% of the activity with fructose 1,6-diphosphate
-
-
sedoheptulose 1,7-bisphosphate
glycerone phosphate + D-erythrose 4-phosphate
show the reaction diagram
-
20% of the activity with D-fructose 1,6-diphosphate
-
-
sedoheptulose 1,7-bisphosphate
?
show the reaction diagram
-
-
-
-
?
L-glyceraldehyde
L-sorbose
show the reaction diagram
-
-
yield 28%
?
additional information
?
-
-
a trace of activity towards fructose 6-phosphate, deoxyribose 5-phosphate and ribose 5-phosphate
-
-
-
additional information
?
-
-
the partitioning of EC 4.1.2.13 and other glycolytic enzymes, between the fluid and solid phases of cytoplasm can play a fundamental role in the control of glycolysis, the organization of cytoplasm, and cell motility
-
-
-
additional information
?
-
-
role in glycerol biosynthesis
-
-
-
additional information
?
-
-
enzyme binds to heparin and modified heparins
-
-
?
additional information
?
-
-
aldolase A specifically participates in glycolysis, aldolase B specifically participates in gluconeogenic pathway
-
-
-
additional information
?
-
-
enzyme is essential for synthesis of alginate from glucose
-
-
-
additional information
?
-
-
the enzyme is regulated by gibberellin in roots of rice seedlings. The enzyme may regulate the vacuolar H+-ATPase mediated control of cell elongation that determines root length
-
-
-
additional information
?
-
-
FBPA exhibits very low activity toward D-tagatose-1,6-bisphosphate
-
-
-
additional information
?
-
-
no activity of MJ0400-His6 is measured with 10 mM fructose-1-phosphate as a substrate. MJ0400 also acts as an 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, this indicates that MJ0400 is involved in both the carbon metabolism and the shikimate pathway in Methanocaldococcus jannaschii
-
-
-
additional information
?
-
-
similar to other Class II FBA, neither fructose 1-phosphate nor fructose 6-phosphate (up to 50 mM each) act as substrates for both rMtFBA
-
-
-
additional information
?
-
-
enzyme favors D-fructose-1,6-bisphosphate as a substrate over D-fructose-1-phosphate and is unchanged between normoxia and anoxia
-
-
-
additional information
?
-
-
enzyme FruA has a flexible substrate specificity and accepts various aldehydes. It is applcable for synthesis of a number of ketoses using simple aliphatic aldehydes as acceptors in a one-pot reaction system. The yields are quite similar for reactions of which acetaldehyde, propionaldehyde, and butyraldehyde are acceptors
-
-
-
additional information
?
-
no substrate: fructose 1-phosphate, fructose 6-phosphate
-
-
-
additional information
?
-
no substrate: fructose 1-phosphate, fructose 6-phosphate. No additional phosphates activity is observed
-
-
-
additional information
?
-
-
product glycerone phosphate is leaving first followed by dihydroxyacetone phosphate in a uni-bi kinetic scheme
-
-
-
additional information
?
-
-
similar to other Class II FBA, neither fructose 1-phosphate nor fructose 6-phosphate (up to 50 mM each) act as substrates for both rMtFBA
-
-
-
additional information
?
-
no substrate: fructose 1-phosphate, fructose 6-phosphate. No additional phosphates activity is observed
-
-
-
additional information
?
-
no substrate: fructose 1-phosphate, fructose 6-phosphate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
ir
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
P05062
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
P00883
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Q9U9R9
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Q9RHA2
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Q9U5N6
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
D4GYE0
the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde 3-phosphate
show the reaction diagram
-
aldolase is involved in the metabolism of fructose, converting fructose 1-phosphate to dihydroxyacetone phosphate and glyceraldehyde
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Archaeoglobus fulgidus 7324
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Haloferax volcanii DSM 3757
D4GYE0
the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Haloferax mediterranei DSM 1411
-
-
-
?
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
P9WQA3
-
-
r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
-
-
-
r
D-fructose-1,6-bisphosphate
glyceraldehyde-3-phosphate + dihydroxyacetone phosphate
show the reaction diagram
-
-
-
r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
P9WQA3
-
-
r
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
Pyrobaculum neutrophilum, Pyrobaculum neutrophilum DSM 2338
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
-
?
additional information
?
-
-
the partitioning of EC 4.1.2.13 and other glycolytic enzymes, between the fluid and solid phases of cytoplasm can play a fundamental role in the control of glycolysis, the organization of cytoplasm, and cell motility
-
-
-
additional information
?
-
-
role in glycerol biosynthesis
-
-
-
additional information
?
-
-
enzyme binds to heparin and modified heparins
-
-
?
additional information
?
-
-
aldolase A specifically participates in glycolysis, aldolase B specifically participates in gluconeogenic pathway
-
-
-
additional information
?
-
-
enzyme is essential for synthesis of alginate from glucose
-
-
-
additional information
?
-
-
the enzyme is regulated by gibberellin in roots of rice seedlings. The enzyme may regulate the vacuolar H+-ATPase mediated control of cell elongation that determines root length
-
-
-
additional information
?
-
-
no activity of MJ0400-His6 is measured with 10 mM fructose-1-phosphate as a substrate. MJ0400 also acts as an 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, this indicates that MJ0400 is involved in both the carbon metabolism and the shikimate pathway in Methanocaldococcus jannaschii
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
activates
Ca2+
1 mM, 82% increase of activity
Ca2+
-
can restore 10% of enzyme activity after complete inhibition by EDTA treatment (2 mM)
Cd2+
-
can partially restore activity of metal depleted enzyme
Cd2+
1 mM lowers enzyme activity by 90%
Co2+
Anacystis sp., Clostridium sp.
-
loosely bound Fe2+ or Co2+
Co2+
-
completely dependent on CoCl2. Maximal activity at 0.75 mM
Co2+
-
no effect
Co2+
-
restores activity after EDTA treatment
Co2+
-
activates
Co2+
-
activates
Co2+
-
better cosubstrate than Zn2+
Co2+
-
best divalent cation, optimal concentration: 0.2 mM
Co2+
optimal metal ion
Co2+
-
the quaternary structure reveals a tetramer composed of two dimers related by a 2-fold axis. Taq FBP aldolase subunits exhibit two distinct conformational states corresponding to loop regions that are in either open or closed position with respect to the active site. Loop closure remodels the disposition of chelating active site histidine residues. In subunits corresponding to the open conformation, the metal cofactor, Co2+, is sequestered in the active site, whereas for subunits in the closed conformation, the metal cation exchanges between two mutually exclusive binding loci, corresponding to a site at the active site surface and an interior site vicinal to the metal-binding site in the open conformation
Co2+
1 mM, 63% increase of activity
Co2+
-
addition of only Co2+ and Zn2+ can recover the activity to higher than half of the original
Co2+
the enzyme activity increases 2.5times in the presence of Co2+
Co2+
-
can restore 20% of enzyme activity after complete inhibition by EDTA treatment (2 mM)
Co2+
1 mM, 128% of initial activity activity; 1 mM, 131% of initial activity activity
Cu2+
-
stimulates
Cu2+
-
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Cu2+
1 mM lowers enzyme activity by 80%
Fe2+
Anacystis sp., Clostridium sp.
-
loosely bound Fe2+ or Co2+
Fe2+
-
maximal activity only when both 8 mM Cys and 0.1 mM Fe2+ are present. Fe3+ or Mn2+ can replace Fe2+
Fe2+
-
no effect
Fe2+
-
activates
Fe2+
-
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Fe2+
-
optimum aldolase activity (137%) is observed with 1.0 mM Fe2+ concentration. Inhibition at concentrations above 1.0 mM. Activity of the enzyme completely inhibited by EDTA (2 mM) can be completely restored by Fe2+
Fe3+
-
maximal activity only when both 8 mM Cys and 0.1 mM Fe2+ are present. Fe3+ or Mn2+ can replace Fe2+
FeSO4
the enzyme requires divalent cation for activity. The highest activity is obtained with MnCl2 (100%, 50 U/mg), which can be partially replaced by FeSO4 (40% residual activity)
K+
Anacystis sp., Clostridium sp.
-
stimulates
K+
-
no effect
K+
-
stimulates
K+
-
stimulates
K+
-
stimulates
K+
-
no effect
K+
-
no effect
K+
-
enhances activity of aldolase II
K+
-
the enzyme is activated up to 5.5fold by the addition of 500 mM KCl
K+
1 mM, 30% increase of activity
KCl
highest activity at 1 mM KCl
KCl
-
the enzyme activity is enhanced by increasing KCl and NaCl concentrations. Optimum activity is diaplayed in 2.5 M KCl, while that in equimolar NaCl is lower. However, aldolase is less active in NH4CI and LiCI
KCl
-
aldolase activity increases with an increasing concentration of KCl. At 4.0 M KCl concentration, activity is 2.5 times that at 0.5 M KCl concentration. Enzyme activity is appreciable even in the absence of added salt
LiCl
-
the enzyme activity is enhanced by increasing KCl and NaCl concentrations. Optimum activity is diaplayed in 2.5 M KCl, while that in equimolar NaCl is lower. However, aldolase is less active in NH4CI and LiCI
Mg2+
-
no effect
Mg2+
-
no effect
Mg2+
-
activates
Mg2+
-
required
Mg2+
-
restores activity after inhibition with EDTA
Mg2+
-
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Mg2+
the glycerone phosphate group coordinates three Mg2+ ions (Mg2Mg4)
Mn2+
-
maximal activity only when both 8 mM Cys and 0.1 mM Fe2+ are present. Fe3+ or Mn2+ can replace Fe2+
Mn2+
-
activates
Mn2+
-
no effect
Mn2+
-
can partially restore activity of metal depleted enzyme
Mn2+
-
restores activity after EDTA treatment
Mn2+
-
activates
Mn2+
-
restores activity after inhibition with EDTA
Mn2+
-
1 mM, the enzyme is dependent on Mn2+
Mn2+
-
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Mn2+
1 mM, 148% of inital activity; 1 mM, 156% of inital activity
Na+
-
stimulates
Na+
-
enhances activity of aldolase II
NaCl
-
the enzyme activity is enhanced by increasing KCl and NaCl concentrations. Optimum activity is diaplayed in 2.5 M KCl, while that in equimolar NaCl is lower. However, aldolase is less active in NH4CI and LiCI
NH4+
Anacystis sp., Clostridium sp.
-
stimulates
NH4+
-
stimulates
NH4+
-
stimulates
NH4Cl
-
the enzyme activity is enhanced by increasing KCl and NaCl concentrations. Optimum activity is diaplayed in 2.5 M KCl, while that in equimolar NaCl is lower. However, aldolase is less active in NH4CI and LiCI
Ni2+
-
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Rb+
-
enhances activity of aldolase II
Zn2+
-
no effect
Zn2+
-
no effect
Zn2+
-
the function appears to be the polarization of the C=O bound of glycerone phosphate. Each subunit of the dimer binds one Zn2+
Zn2+
-
activates
Zn2+
-
activates
Zn2+
can replace Co2+ at a limited rate
Zn2+
the native recombinant enzyme is zinc-dependent, contains 0.5 Zn2+ per monomer
Zn2+
-
the EDTA-inhibited activity can be restored to 109% of the original activity by the addition of 1 mM ZnSO4
Zn2+
1 mM, 189% increase of activity
Zn2+
-
dependent, the active site contains a zinc ion
Zn2+
-
addition of only Co2+ and Zn2+ can recover the activity to higher than half of the original
Zn2+
FBPA belongs to the class II zinc-dependent aldolase family, each subunit contains a Zn2+ cofactor
Zn2+
-
dependent
Zn2+
1 mM lowers enzyme activity by 60%
Zn2+
-
contains 0.97 zinc atoms per subunit
Zn2+
-
contains 0.83 zinc atoms per subunit
Zn2+
-
contains 0.49 zinc atoms per subunit
Zn2+
-
contains 0.16 zinc atoms per subunit
MnCl2
the enzyme requires divalent cation for activity. The highest activity is obtained with MnCl2 (100%, 50 U/mg), which can be partially replaced by FeSO4 (40% residual activity)
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
-
class I fructose diphosphate aldolases, Schiff-base forming, does not require a metal ion
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
-
class I fructose diphosphate aldolases, Schiff-base forming, does not require a metal ion
additional information
-
no metal requirement
additional information
-
FBPasealdolase complex is located on a actinin of the Z-line. The stability of the complex is regulated by calcium ions. Elevated calcium concentration decreases association constant of FBPasealdolase and FBPase-alpha-actinin complex, causes fast dissociation of FBPase from the Z-line and slow accumulation of aldolase within the I-band and M-line. Release of Ca2+ during muscle contraction might result, simultaneously, in the inhibition of glyconeogenesis and in the acceleration of glycolysis
additional information
-
Mg2+ has no effect
additional information
-
not dependent on Zn2+
additional information
-
1 mM Fe2+, Ca2+, or Mg2+ fail to recover the activity lost by 0.5 mM EDTA application and 0.5 mM cysteine and 1 mM 2-mercaptoethanol have almost no effect on the enzyme activity
additional information
Cd2+ has no effect on activity
additional information
Mg2+ or Ca2+ have no effect on enzme activity
additional information
-
the addition of Co2+ to the purified Bacillus cereus aldolase does not increase the relatively low specific activity of this recombinant enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
50% inhibition at 2.1 mM at 37C, 50% inhibition at 1.9 mM at 5C
(NH4)2SO4
-
50% inhibition at 6.2 mM at 37C, 50% inhibition at 5.27 mM at 5C
([3-hydroxy-2-oxo-4-[(phosphonomethoxy)methyl]pyridin-1(2H)-yl]methyl)phosphonic acid
-
-
([3-hydroxy-2-oxo-4-[2-(phosphonooxy)ethyl]pyridin-1(2H)-yl]methyl)phosphonic acid
-
-
([3-hydroxy-4-[(1R)-1-hydroxy-2-(phosphonooxy)ethyl]-2-oxopyridin-1(2H)-yl]methyl)phosphonic acid
-
-
([3-hydroxy-4-[(1S)-1-hydroxy-2-(phosphonooxy)ethyl]-2-oxopyridin-1(2H)-yl]methyl)phosphonic acid
-
-
([4,5-dihydroxy-6-[2-(phosphonooxy)ethyl]pyridin-3-yl]methyl)phosphonic acid
-
-
1,10-phenanthroline
-
aldolase class II
1,10-phenanthroline
-
2 mM, 85% inhibition
1-hydroxy-2-naphthaldehyde 6-phosphate
-
slow-binding
2,2'-bipyridyl
-
2 mM, 76% inhibition
2,2'-dipyridyl
-
aldolase class II
2,4-Dihydroxybenzaldehyde 4-phosphate
-
-
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl dihydrogen phosphate
-
-
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl phosphate
-
-
2-carboxy-6-(phosphonomethyl)pyridinium chloride
-
metal-chelating inhibitor
2-hydroxy-2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl dihydrogen phosphate
-
-
2-mercaptoethanol
-
5 mM, 19% loss of activity
2-mercaptoethanol
-
10 mM, 38% residual activity
2-oxo-2-[(phenylsulfonyl)amino]ethyl phosphate
-
-
2-oxoglutarate
-
-
2-propanol
-
at 12.5% (v/v) remaining activity, 69.99%, and 25% (v/v) remaining activity, 3.72%
2-[(methylsulfonyl)amino]-2-oxoethyl phosphate
-
-
2-[(trihydroxyphosphoranyl)oxy]acetohydrazide
-
-
2-[hydroxy(3-hydroxypropyl)amino]-2-oxoethyl dihydrogen phosphate
-
-
2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
-
-
3-phosphoglycerate
-
-
3-[hydroxy[(phosphonooxy)acetyl]amino]propyl dihydrogen phosphate
-
-
4-Hydroxybenzaldehyde phosphate
-
competitive
-
5,5-dithiobis(2-nitrobenzoic acid)
-
1 mM, complete inhibition
-
5-chloro-8-hydroxyquinoline
-
non-competitive (mixed type)
5-formyl-6-hydroxynaphthalen-2-yl dihydrogen phosphate
-
1 mM, 15 min incubation time, 80% residual activity
5-formyl-6-hydroxynaphthalen-2-yl dihydrogen phosphate
-
5 mM, 15 min incubation time, no residual activity
6-phosphogluconate
-
-
8-hydroxyquinoline
-
aldolase class II
8-hydroxyquinoline
-
-
ADP
-
-
ADP
-
50% inhibition at 1.6 mM at 37C, 50% inhibition at 1.7 mM at 5C
ADP
-
50% inhibition at 2.7 mM at 37C, 50% inhibition at 5.4 mM at 5C
ADP
-
competitive
ADP
1 mM, 47% residual activity; 1 mM, 58% residual activity
Agaricic acid
-
50% inhibition at 0.03 mM
alpha-glycerophosphate
-
-
AMP
-
MgAMP
AMP
-
50% inhibition at 2.3 mM at 37C, 50% inhibition at 2.6 mM at 5C
AMP
-
50% inhibition at 4.5 mM at 37C, 50% inhibition at 6.0 mM at 5C
AMP
-
strong allosteric inhibition. I0.5: 0.00023 mM
AMP
-
competitive
ascorbic acid
-
-
ATP
-
-
ATP
-
50% inhibition at 1.4 mM at 37C, 50% inhibition at 1.1 mM at 5C
ATP
-
50% inhibition at 2.1 mM at 37C, 50% inhibition at 2.1 mM at 5C
ATP
1 mM, 34% residual activity; 1 mM, 39% residual activity
Benzene
-
at 12.5% (v/v) remaining activity, 88.94%, and 25% (v/v) remaining activity, 88.94%
Bromoacetate
-
-
butanol
-
-
Cd2+
1 mM, no residual activity; 1 mM, no residual activity
Chelators
-
-
-
citrate
-
-
citrate
-
50% inhibition at 2.4 mM at 37C, 50% inhibition at 1.9 mM at 5C
citrate
-
50% inhibition at 2.7 mM at 37C, 50% inhibition at 3.4 mM at 5C
Cr3+
1 mM, 36% decrease of activity
Cu2+
-
complete inhibition of aldolase II above 0.5 mM
Cu2+
1 mM, 57% decrease of activity
Cu2+
1 mM, 3% residual activity; 1 mM, 5% residual activity
CuCl2
-
1 mM, complete inhibition
CuSO4
-
0.02 mM, inactivation
Cys
-
inhibits aldolase II above 0.8 mM
D-erythrose 4-phosphate
-
competitive
D-Erythrulose 1-phosphate
-
slow reversible
D-fructose 1,6-bisphosphate
substrate inhibition; substrate inhibition
D-glucitol 1,6-bisphosphate
-
competitive inhibitor
D-glucitol 1,6-bisphosphate
-
competitive inhibitor, better inhibitor
D-hexitol-1,6-bisphosphate
-
-
D-mannitol 1,6-bisphosphate
-
competitive inhibitor, better inhibitor
D-mannitol 1,6-bisphosphate
-
competitive inhibitor
D-mannitol-1,6-bisphosphate
-
competitive inhibitor
D-ribulose 1,5-bisphosphate
-
-
D-tagatose 1,6-bisphosphate
competitive inhibitor
dihydroxyacetone phosphate
-
-
dihydroxyacetone phosphate
-
competitive with fructose 1,6-bisphosphate
dimethylsulfoxid
-
at 12.5% (v/v) remaining activity, 131.26%, and 25% (v/v) remaining activity, 133.2%
diphosphate
-
-
diphosphate
-
-
EDTA
-
insensitive
EDTA
-
inhibition is fully reversed by a divalent metal ion
EDTA
-
activity restored after addition of Zn2+, Co2+ or Mn2+
EDTA
-
insensitive
EDTA
-
insensitive
EDTA
-
insensitive
EDTA
-
insensitive
EDTA
1 mM, completely abolishes activity
EDTA
-
0.67 mM, complete inhibition
EDTA
-
0.025 mM and above, no residual activity
EDTA
1 mM, complete inhibition
EDTA
complete inhibition at 1 mM
EDTA
-
the specific activity of the Bacillus cereus aldolase is partially restored after EDTA inactivation by Co2+ and Cd2+, as well as Zn2+, but not significantly restored by Cu2+, Mn2+, Mg2+, or Ni2+
EDTA
-
the activity of the EDTA-inactivated enzyme increases more than 6fold upon the addition of 0.002 mM Zn2+ and increases by a factor 2 with the addition of 0.002 mM Co2+. The addition of Cu2+, Ni2+, Cd2+, Mn2+, or Mg2+ does not reactivate the enzyme significantly
EDTA
-
the specific activity of the recombinant Pseudomonas aeruginosa aldolase is 5.5times higher after inactivation by EDTA followed by the addition of 0.02 mM cobalt chloride, and increases more than 2fold after EDTA inactivation followed by the addition of 0.1 mM manganese(II)-chloride
EDTA
2 mM, complete inhibition of activity, which could be reversed by the addition of Mn2+ (3 mM)
EDTA
-
1 mM, 7% inhibition
EDTA
-
2 mM, complete inhibition. Activity can be completely restored only by Fe2+. Other divalent metal ions such as Mn2+, Mg2+, and Zn2+ have no effect. Co2+ and Ca2+ can restore 20% and 10%, respectively, of enzyme activity
EDTA
1 mM, no residual activity; 1 mM, no residual activity
erythrose 4-phosphate
-
-
ethanol
-
at 12.5% (v/v) remaining activity, 79.19%, and 25% (v/v) remaining activity, 33.41%
ethyl acetate
-
at 12.5% (v/v) remaining activity, 71.96%, and 25% (v/v) remaining activity, 41.62%
Fe2+
-
optimum aldolase activity (137%) is observed with 1.0 mM Fe2+ concentration. Inhibition at concentrations baove 1.0 mM
Fe2+
1 mM, 15% residual activity; 1 mM, 18% residual activity
Fluorescein 5'-isothiocyanate
results in a minimal loss of enzyme activity
fructose 6-phosphate
-
-
glucose 1-phosphate
-
-
glucose 1-phosphate
-
-
glucose 6-phosphate
-
-
glutathione
-
10 mM, 62% residual activity
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
non-competitive inhibitor
glycerol
-
at 20% (v/v) reduced enzyme activity by 65%
Glycerol 2,3-diphosphate
-
-
glycerone phosphate
-
inhibition in presence of glycerone phosphate and NaBH4
glycerone phosphate
-
inhibition in presence of glycerone phosphate and NaBH4
glycerone phosphate
-
-
glycerone phosphate
-
-
glycerone phosphate
-
inhibition in presence of glycerone phosphate and NaBH4
glyoxylate
-
-
hexane
-
at 12.5% (v/v) remaining activity, 98.25%, and 25% (v/v) remaining activity, 92.22%
hexitol-1,6-bisphosphate
-
strong competitive inhibitor
HgCl2
-
1 mM, complete inhibition
hydrogen peroxide
-
inhibitory at 0.25%, at pH 7
Hydroquinone diphosphate
-
competitive
IMP
-
-
IMP
-
50% inhibition at 1.3 mM at 37C, 50% inhibition at 1.3 mM at 5C
IMP
-
50% inhibition at 4.2 mM at 37C, 50% inhibition at 8.5 mM at 5C
iodoacetamide
-
76% residual activity at 10 mM
iodoacetate
-
10 mM, 28% loss of activity
iodoacetate
-
1 mM, 46% inhibition
KCl
-
50% inhibition at 38.2 mM at 37C, 50% inhibition at 36.1 mM at 5C
KCl
-
50% inhibition at 111 mM at 37C, 50% inhibition at 63.3 mM at 5C
L-cysteine
-
10 mM, complete inhibition
Magnesium citrate
-
50% inhibition at 1.9 mM at 37C, 50% inhibition at 2.5 mM at 5C
Magnesium citrate
-
50% inhibition at 9 mM at 37C, 50% inhibition at 2.5 mM at 5C
mannitol-1,6-bis(phosphate)
-
competitive
N'-hydroxy-2-[(trihydroxyphosphoranyl)oxy]ethanimidamide
-
-
N,N-dimethylmethanamide
-
at 12.5% (v/v) remaining activity, 118.40%, and 25% (v/v) remaining activity, 73.93%
N-(3-hydroxypropyl)-glycolohydrazide-bisphosphate
-
fructose-1,6-bisphosphate analogue
N-(3-hydroxypropyl)-glycolohydroxamic acid bisphosphate
-
fructose-1,6-bisphosphate analogue, best results
N-(3-hydroxypropyl)-glycolohydroxamic acid bisphosphate
-
fructose-1,6-bisphosphate analogue, weakly active
N-(3-hydroxypropyl)-glycolohydroxamic acid bisphosphate
-
fructose-1,6-bisphosphate analogue, best results
N-(3-hydroxypropyl)-phosphoglycolohydroxamic acid
-
fructose-1,6-bisphosphate analogue
N-(4-hydroxybutyl)-glycolohydroxamic acid bisphosphate
-
inhibitor attachment has no effect on the plasminogen binding activity of the enzyme but competes with the natural substrate, fructose 1,6-bisphosphate, and substantiates a reaction mechanism associated with metallodependent aldolases involving recruitment of the catalytic zinc ion by the substrate upon active site binding
-
N-hydroxy-2-[(trihydroxyphosphoranyl)oxy]acetamide
-
-
NaBH4
-
in presence of substrate
NaBH4
Chlamydomonas sp.
-
metalloaldolases are indifferent
NaBH4
-
irreversible inactivation
NaBH4
-
inactivation
NaBH4
-
inhibition in presence of glycerone phosphate and NaBH4
NaBH4
-
-
NaBH4
-
in presence of substrate
NaBH4
-
inhibition in presence of glycerone phosphate and NaBH4
NaCl
-
50% inhibition at 14.7 mM at 37C, 50% inhibition at 31 mM at 5C
NaCl
-
50% inhibition at 110 mM at 37C, 50% inhibition at 52 mM at 5C
naphthalene-2,6-bisphosphate
-
strong competitive inhibitor
naphthyl 2,6-bisphosphate
-
competitive
NH4Cl
-
50% inhibition at 51.5 mM at 37C, 50% inhibition at 34.1 mM at 5C
NH4Cl
-
50% inhibition at 166 mM at 37C, 50% inhibition at 40.6 mM at 5C
Ni2+
-
cells stressed by 8 microM Ni(II) for 20 min lose 75% of their FbaA activity. In presence of 8 microM Ni(II), purified FbaA loses 80% of its activity within 2 min. Inhibition is due to Ni(II) binding to a secondary zinc binding site
o-phenanthroline
-
0.06 mM, inactivation
oxaloacetate
-
-
peroxynitrite
-
decrease of Vmax and KM for fructose-1,6-bisphosphate after incubation with peroxynitrite. Tyrosine residues in the carboxyl-terminal region of the aldolase are major targets of nitration. Tyrosine nitration of aldolase A can contribute to an impaired cellular glycolytic activity
phosphate
-
-
phosphate
-
-
phosphate
-
50% inhibition at 1.7 mM at 37C, 50% inhibition at 0.63 mM at 5C
phosphate
-
50% inhibition at 6.1 mM at 37C, 50% inhibition at 1.7 mM at 5C
phosphatidylserine
-
-
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
mixed-type inhibitor
phosphoglycolo hydroxamic acid
-
PGH, i.e. 2-(hydroxyamino)-2-oxoethyl phosphate
phosphoglycolo hydroxamic acid
-
PGH, i.e. 2-(hydroxyamino)-2-oxoethyl phosphate
phosphoglycolo-amidoxime
-
PGA, i.e. 2-amino-2-(hydroxyimino)ethyl phosphate
phosphoglycolo-hydrazide
-
PGHz, i.e. 2-hydrazino-2-oxoethyl phosphate
phosphoglycoloamidoxime
-
dihydroxyacetone phosphate analogue
phosphoglycolohydrazide
-
dihydroxyacetone phosphate analogue
Phosphoglycolohydroxamate
-
-
Phosphoglycolohydroxamate
-
use as a mimic of the hydroxyenolate intermediate- and dihydroxyacetone phosphate-bound form of the enzyme
Polyphosphate
-
-
Propanol
-
-
pyridoxal 5'-phosphate
-
-
pyruvate
-
-
Resorcinol diphosphate
-
competitive
ribose 5-phosphate
-
-
ribose 5-phosphate
-
-
ribose 5-phosphate
-
competitive
sulfhydryl reagents
-
-
suramin
-
50% inhibition at 0.025 mM
tagatose 1,6-bisphosphate
-
-
Toluene
-
at 12.5% (v/v) remaining activity, 89.70%, and 25% (v/v) remaining activity, 91.02%
Zn2+
-
ZnSO4
Zn2+
-
complete inhibition of aldolase II above 0.5 mM
Zn2+
1 mM, 15% residual activity; 1 mM, 8% residual activity
[(3-hydroxy-2-oxopyridin-1(2H)-yl)methyl]phosphonic acid
-
-
[2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl]phosphonic acid
-
-
[[(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)methoxy]methyl]phosphonic acid
-
-
[[3-hydroxy-2-oxo-4-(2-phosphonoethyl)pyridin-1(2H)-yl]methyl]phosphonic acid
-
-
additional information
-
-
-
additional information
-
EDTA has no effect
-
additional information
-
EDTA has no effect
-
additional information
-
all methyl 4-oxo-2-butenoates, 3-hydroxy-2-pyrrolones, 1,4-bezoxazines and compounds containing 4-quinolone fragment does not inhibit rMtFBA
-
additional information
high pH, high temperature, and ionic detergents either inhibit or prevent the reaction of fluorescein 5'-isothiocyanate with aldolase. Certain metabolites (ATP, ADP, CTP, GTP, FBP) and erythrosin B also inhibited the fluorescein 5'-isothiocyanate modification of aldolase
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
sulfhydryl compound such as 2-mercaptoethanol, activates the C-His-rMtFBA activity slightly, 15%
2-oxoglutarate
-
enhances D-fructose 1,6-bisphosphate-cleavage activity, fructose 1-phosphate-cleavage activity is unaffected
arsenate
-
causes further enhancement of enzyme activity when added iin 1-10 mM amounts in the standard assay medium containing KCl. Activity with 12 mM arsenate, is threefold higher than the original aldolase activity
citrate
-
enhances activity
Cys
-
maximal activity only when both 8 mM Cys and 0.1 mM Fe2+ are present. Fe3+ or Mn2+ can replace Fe2+
cysteine
highest activity at 1 mM cysteine
cysteine
-
1 mM, 1.3fold activation
D-glucose
-
about 60% increase of activity
diphosphate
-
causes further enhancement of enzyme activity when added in 1-10 mM amounts in the standard assay medium containing KCl
dithiothreitol
-
sulfhydryl compound such as dithiothreitol, activates the C-His-rMtFBA activity slightly, 25%
dithiothreitol
-
required
dithiothreitol
-
up to 5 mM, enhances enzyme activity twofold
Nonidet-P40
-
0.5% w/v, enhances activity by 34%
phosphate
-
causes further enhancement of enzyme activity when added in 1-10 mM amounts in the standard assay medium containing KCl
phosphoenolpyruvate
-
enhances D-fructose 1,6-bisphosphate-cleavage activity, fructose 1-phosphate-cleavage activity is unaffected
reduced glutathione
-
1 mM, 1.4fold activation
sn-glycerol 3-phosphate
-
enhances D-fructose 1,6-bisphosphate-cleavage activity, fructose 1-phosphate-cleavage activity is unaffected
Triton X-100
-
0.5% w/v, enhances activity by 31%
Triton X-100
-
increased enzyme activity by 33%
Tween 20
-
0.5% w/v, enhances activity by 88%
Tween 80
-
0.5% w/v, enhances activity by 39%
ethanol
-
10% w/v, increases activity by 24%
additional information
-
1 mM PMSF has no effect on the enzyme activity
-
additional information
-
citrate or phosphoenolpyruvate show no effect on the FBP activity of MJ0400-His6
-
additional information
-
AMP, ADP or glucose (2 mM) have no effect on activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00016
D-fructose 1,6-bisphosphate
-
-
0.00018
D-fructose 1,6-bisphosphate
-
pH 7.2, 25C, anoxic liver preparation
0.00024
D-fructose 1,6-bisphosphate
-
pH 7.2, 25C, normoxic liver preparation
0.0003
D-fructose 1,6-bisphosphate
-
-
0.000547
D-fructose 1,6-bisphosphate
-
-
0.00065
D-fructose 1,6-bisphosphate
-
enzyme form I
0.00084
D-fructose 1,6-bisphosphate
-
30C, aldolase B
0.0009
D-fructose 1,6-bisphosphate
-
pH 7.3, 37C
0.001
D-fructose 1,6-bisphosphate
-
-
0.0011
D-fructose 1,6-bisphosphate
-
cytosolic enzyme
0.0011
D-fructose 1,6-bisphosphate
-
30C, AB_All mutant
0.00113
D-fructose 1,6-bisphosphate
-
at 33C
0.0013
D-fructose 1,6-bisphosphate
-
pH 7.3, 37C
0.00145
D-fructose 1,6-bisphosphate
-
pH 7.3, 5C
0.0016
D-fructose 1,6-bisphosphate
-
cytosolic enzyme
0.0016
D-fructose 1,6-bisphosphate
-
liver enzyme,
0.0017
D-fructose 1,6-bisphosphate
-
pH 7.4, 10C, wild-type enzyme
0.0017
D-fructose 1,6-bisphosphate
-
at pH 7.5 and 25C, in the absence of Zn2+
0.0017
D-fructose 1,6-bisphosphate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5), at 25C
0.002
D-fructose 1,6-bisphosphate
-
liver
0.002
D-fructose 1,6-bisphosphate
-
-
0.002
D-fructose 1,6-bisphosphate
-
cytosolic enzyme
0.002
D-fructose 1,6-bisphosphate
-
at pH 7.5 and 25C
0.0023
D-fructose 1,6-bisphosphate
-
cytosolic enzyme
0.0023
D-fructose 1,6-bisphosphate
wild-type enzyme, 22C
0.0024
D-fructose 1,6-bisphosphate
-
pH 7.4, 30C, wild-type enzyme
0.00245
D-fructose 1,6-bisphosphate
-
5C
0.0027
D-fructose 1,6-bisphosphate
-
mutant aldolase C Y363S
0.0028
D-fructose 1,6-bisphosphate
-
pH 7.4, 10C, enzyme from patients with intolerance
0.0035
D-fructose 1,6-bisphosphate
-
recombinant enzyme
0.0037
D-fructose 1,6-bisphosphate
-
-
0.004
D-fructose 1,6-bisphosphate
-
wild-type, 22C, pH 7.6
0.00411
D-fructose 1,6-bisphosphate
-
pH 7.3, 5C
0.0042
D-fructose 1,6-bisphosphate
-
mutant enzyme D33N
0.0043
D-fructose 1,6-bisphosphate
-
-
0.0048
D-fructose 1,6-bisphosphate
-
non-muscle-type enzyme
0.005
D-fructose 1,6-bisphosphate
-
recombinant non-muscle-type enzyme
0.0051
D-fructose 1,6-bisphosphate
-
native wild type enzyme
0.0052
D-fructose 1,6-bisphosphate
in the presence of 0.02 mM Co2+, at substrate concentrations of 0.008-0.5 mM, at pH 7.5, 30C
0.0055
D-fructose 1,6-bisphosphate
W147R mutant, 22C
0.0056
D-fructose 1,6-bisphosphate
-
plastidic enzyme
0.0058
D-fructose 1,6-bisphosphate
-
cytosolic enzyme
0.0059
D-fructose 1,6-bisphosphate
-
L256P, 22C, pH 7.6
0.006
D-fructose 1,6-bisphosphate
-
-
0.0061
D-fructose 1,6-bisphosphate
-
mutant enzyme E187A
0.007
D-fructose 1,6-bisphosphate
-
pH 8, class I aldolase, recombinant enzyme
0.0071
D-fructose 1,6-bisphosphate
-
-
0.0073
D-fructose 1,6-bisphosphate
L256P mutant, 22C
0.008
D-fructose 1,6-bisphosphate
-
chloroplastic enzyme
0.008
D-fructose 1,6-bisphosphate
-
pH 7.5, class II aldolase, purified enzyme; pH 7.5, class II aldolase, recombinant enzyme
0.0081
D-fructose 1,6-bisphosphate
-
-
0.0083
D-fructose 1,6-bisphosphate
-
chloroplastic enzyme
0.0084
D-fructose 1,6-bisphosphate
-
mutant enzyme D33S
0.0085
D-fructose 1,6-bisphosphate
-
pH 7.4, 30C, enzyme from patients with intolerance
0.0088
D-fructose 1,6-bisphosphate
-
pH 7.6
0.0089
D-fructose 1,6-bisphosphate
-
aldolase C
0.009
D-fructose 1,6-bisphosphate
-
pH 8, class I aldolase, purified enzyme
0.0091
D-fructose 1,6-bisphosphate
-
chloroplastic enzyme
0.0091
D-fructose 1,6-bisphosphate
Q354E mutant, 22C
0.0092
D-fructose 1,6-bisphosphate
-
pH 7.6, native enzyme
0.0095
D-fructose 1,6-bisphosphate
-
30C, aldolase A
0.0095
D-fructose 1,6-bisphosphate
-
at 30C
0.01
D-fructose 1,6-bisphosphate
-
-
0.0102
D-fructose 1,6-bisphosphate
-
30C, H156E mutant
0.0107
D-fructose 1,6-bisphosphate
-
-
0.012
D-fructose 1,6-bisphosphate
-
aldolase B
0.012
D-fructose 1,6-bisphosphate
-
aldolase I
0.012
D-fructose 1,6-bisphosphate
-
wild-type and mutants, pH 7.4
0.013
D-fructose 1,6-bisphosphate
-
aldolase C
0.013
D-fructose 1,6-bisphosphate
-
wild-type enzyme
0.0134
D-fructose 1,6-bisphosphate
-
enzyme form II
0.0134
D-fructose 1,6-bisphosphate
-
mutant enzyme E187Q
0.0138
D-fructose 1,6-bisphosphate
-
pH 7.6
0.0146
D-fructose 1,6-bisphosphate
-
native enzyme, in Tris-HCl buffer (40 mM, pH 8.0), at 25C
0.015
D-fructose 1,6-bisphosphate
-
-
0.016
D-fructose 1,6-bisphosphate
-
recombinant muscle-type enzyme
0.016
D-fructose 1,6-bisphosphate
mutant enzyme D255A, in 50 mM K+-HEPES (pH 7.5), at 25C
0.0167
D-fructose 1,6-bisphosphate
-
pH 7.5, 30C
0.0168
D-fructose 1,6-bisphosphate
-
pH 7.6, recombinant enzyme
0.018
D-fructose 1,6-bisphosphate
-
muscle-type enzyme
0.018
D-fructose 1,6-bisphosphate
in the absence of Co2+, at pH 7.5, 30C
0.0188
D-fructose 1,6-bisphosphate
-
recombinant fusion protein DLF, in Tris-HCl buffer (40 mM, pH 8.0), at 25C
0.02
D-fructose 1,6-bisphosphate
-
enzyme from cytoplasm and chloroplast
0.02
D-fructose 1,6-bisphosphate
-
E182A mutant, 30C
0.02
D-fructose 1,6-bisphosphate
pH 7.3, 28C
0.02
D-fructose 1,6-bisphosphate
-
-
0.0204
D-fructose 1,6-bisphosphate
-
mutant enzyme K146M
0.0205
D-fructose 1,6-bisphosphate
-
-
0.022
D-fructose 1,6-bisphosphate
-
-
0.022
D-fructose 1,6-bisphosphate
-
A337V, 22C, pH 7.6
0.025
D-fructose 1,6-bisphosphate
-
-
0.027
D-fructose 1,6-bisphosphate
-
A149P, 22C, pH 7.6
0.0279
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30C
0.03
D-fructose 1,6-bisphosphate
-
at pH 7.5 and pH 8.0
0.032
D-fructose 1,6-bisphosphate
N334K mutant, 22C
0.035
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30C
0.0401
D-fructose 1,6-bisphosphate
-
pH 9.3
0.0412
D-fructose 1,6-bisphosphate
-
mutant enzyme K107M
0.045
D-fructose 1,6-bisphosphate
-
-
0.0459
D-fructose 1,6-bisphosphate
-
pH 5.5
0.047
D-fructose 1,6-bisphosphate
-
W147R, 22C, pH 7.6
0.049
D-fructose 1,6-bisphosphate
-
pH 7.6
0.05
D-fructose 1,6-bisphosphate
-
at 30C in 50 mM Tris-HCl, 0.1 M potassium acetate buffer (pH 8.0)
0.051
D-fructose 1,6-bisphosphate
-
at pH 7.8
0.051
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30C
0.0519
D-fructose 1,6-bisphosphate
wild-type enzyme
0.052
D-fructose 1,6-bisphosphate
-
aldolase A
0.055
D-fructose 1,6-bisphosphate
-
-
0.0552
D-fructose 1,6-bisphosphate
-
pH 9.3
0.0566
D-fructose 1,6-bisphosphate
mutant enzyme G346S
0.06
D-fructose 1,6-bisphosphate
-
muscle
0.0656
D-fructose 1,6-bisphosphate
-
pH 5.5
0.0728
D-fructose 1,6-bisphosphate
-
pH 5.5
0.074
D-fructose 1,6-bisphosphate
-
-
0.0777
D-fructose 1,6-bisphosphate
-
pH 9.2
0.08
D-fructose 1,6-bisphosphate
-
aldolase class II
0.1
D-fructose 1,6-bisphosphate
-
-
0.1
D-fructose 1,6-bisphosphate
-
at 48C
0.105
D-fructose 1,6-bisphosphate
mutant enzyme E206K
0.12
D-fructose 1,6-bisphosphate
-
-
0.13
D-fructose 1,6-bisphosphate
-
E174A mutant, 30C
0.14
D-fructose 1,6-bisphosphate
-
30C
0.15
D-fructose 1,6-bisphosphate
-
immobilized enzyme
0.15
D-fructose 1,6-bisphosphate
-
mutant enzyme K107M
0.15
D-fructose 1,6-bisphosphate
-
30C
0.16
D-fructose 1,6-bisphosphate
-
-
0.16
D-fructose 1,6-bisphosphate
pH 7.6, 50C
0.1613
D-fructose 1,6-bisphosphate
-
-
0.17
D-fructose 1,6-bisphosphate
-
wild-type enzyme, 30C
0.175
D-fructose 1,6-bisphosphate
-
aldolase II
0.18
D-fructose 1,6-bisphosphate
-
30C, D109A mutant
0.19
D-fructose 1,6-bisphosphate
-
30C, wild-type enzyme
0.2
D-fructose 1,6-bisphosphate
-
-
0.22
D-fructose 1,6-bisphosphate
-
Q59A mutant, 30C
0.24
D-fructose 1,6-bisphosphate
pH 7.5, 42C
0.3
D-fructose 1,6-bisphosphate
-
E181A mutant, 30C
0.3
D-fructose 1,6-bisphosphate
-
-
0.305
D-fructose 1,6-bisphosphate
70C, pH 6.5
0.33
D-fructose 1,6-bisphosphate
-
R303W, 22C, pH 7.6
0.37
D-fructose 1,6-bisphosphate
-
30C, N286D mutant
0.38
D-fructose 1,6-bisphosphate
-
K325A mutant, 30C
0.38
D-fructose 1,6-bisphosphate
-
pH 7.5, 37C
0.43
D-fructose 1,6-bisphosphate
-
S61T mutant, 30C
0.45
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30C
0.576
D-fructose 1,6-bisphosphate
in 50 mM Tris-HCl buffer at pH 8.5 and 60C
0.77
D-fructose 1,6-bisphosphate
-
30C, D290A mutant
0.9
D-fructose 1,6-bisphosphate
-
N35A mutant, 30C
0.92
D-fructose 1,6-bisphosphate
-
30C, D329A mutant
0.94
D-fructose 1,6-bisphosphate
-
30C, D144A mutant
1
D-fructose 1,6-bisphosphate
-
30C, D288A mutant
1.07
D-fructose 1,6-bisphosphate
-
30C, N286A mutant
1.1
D-fructose 1,6-bisphosphate
in the presence of 0.02 mM Co2+, at substrate concentrations of 0.5-1.5 mM, at pH 7.5, 30C
1.8
D-fructose 1,6-bisphosphate
-
-
2
D-fructose 1,6-bisphosphate
-
-
2
D-fructose 1,6-bisphosphate
-
pH 7.5, 37C
2
D-fructose 1,6-bisphosphate
pH 7.8, 55C
2.7
D-fructose 1,6-bisphosphate
-
S61A mutant, 30C
4.2
D-fructose 1,6-bisphosphate
-
50C, pH not specified in the publication
5.1
D-fructose 1,6-bisphosphate
-
native recombinant enzyme, pH 7.6, 22C
5.7
D-fructose 1,6-bisphosphate
-
E189A mutant, pH 7.6, 22C
6.2
D-fructose 1,6-bisphosphate
-
E187A mutant, pH 7.6, 22C
10.9
D-fructose 1,6-bisphosphate
-
E189Q mutant, pH 7.6, 22C
13.4
D-fructose 1,6-bisphosphate
-
E187Q mutant, pH 7.6, 22C
20
D-fructose 1,6-bisphosphate
-
-
0.0017
D-Fructose 1-phosphate
W147R mutant, 22C
0.00173
D-Fructose 1-phosphate
L256P mutant, 22C
0.0022
D-Fructose 1-phosphate
wild-type enzyme, 22C
0.0024
D-Fructose 1-phosphate
-
wild-type, 22C, pH 7.6
0.0033
D-Fructose 1-phosphate
-
L256P, 22C, pH 7.6
0.0098
D-Fructose 1-phosphate
-
A149P, 22C, pH 7.6
0.022
D-Fructose 1-phosphate
N334K mutant, 22C
0.024
D-Fructose 1-phosphate
-
A337V, 22C, pH 7.6
0.0266
D-Fructose 1-phosphate
-
W147R, 22C, pH 7.6
0.05
D-Fructose 1-phosphate
Q354E mutant, 22C
0.24
D-Fructose 1-phosphate
-
pH 7.4, 10C, wild-type enzyme
0.723
D-Fructose 1-phosphate
-
30C, aldolase B
0.88
D-Fructose 1-phosphate
-
pH 7.4, 30C, wild-type enzyme
2.6
D-Fructose 1-phosphate
-
30C, AB_All mutant
4.2
D-Fructose 1-phosphate
-
pH 7.4, 10C, enzyme from patients with intolerance
16
D-Fructose 1-phosphate
-
-
16.4
D-Fructose 1-phosphate
-
pH 7.4, 30C, enzyme from patients with intolerance
28
D-Fructose 1-phosphate
-
pH 7.5, 37C
39.8
D-Fructose 1-phosphate
-
30C, aldolase A
40
D-Fructose 1-phosphate
-
at 30C
0.01503
D-fructose-1,6-bisphosphate
-
purified C-His-rMtFBA, indicates that the extra five histidine residues in C-His-rMtFBA has negligible effects on the kinetic properties of the enzyme
0.01598
D-fructose-1,6-bisphosphate
-
purified native-rMtFBA
0.018
D-fructose-1,6-bisphosphate
-
mutant E169A, pH 7.8, 22C
0.021
D-fructose-1,6-bisphosphate
-
mutant G167A/G166A, pH 7.8, 22C; mutant G167A, pH 7.8, 22C
0.0279
D-fructose-1,6-bisphosphate
-
pH 7.3, 28C
0.03
D-fructose-1,6-bisphosphate
-
mutant E168A, pH 7.8, 22C
0.035
D-fructose-1,6-bisphosphate
-
pH 7.3, 28C
0.04
D-fructose-1,6-bisphosphate
-
wild-type, pH 7.8, 22C
0.05
D-fructose-1,6-bisphosphate
-
-
0.051
D-fructose-1,6-bisphosphate
-
pH 7.3, 28C
0.055
D-fructose-1,6-bisphosphate
-
-
0.18
D-fructose-1,6-bisphosphate
-
mutant D276A, pH 7.8, 22C
0.43
D-fructose-1,6-bisphosphate
-
at 50C
0.45
D-fructose-1,6-bisphosphate
-
-
0.45
D-fructose-1,6-bisphosphate
-
pH 7.3, 28C
0.052
D-glyceraldehyde 3-phosphate
pH 6.5, 70C
0.19
D-glyceraldehyde 3-phosphate
pH 8.0, 48C, wild-type enzyme
0.25
D-glyceraldehyde 3-phosphate
pH 7.8, 55C
0.34
D-glyceraldehyde 3-phosphate
pH 8.0, 48C, mutant enzyme Y348F
0.58
D-glyceraldehyde 3-phosphate
pH 7.6, 50C
1.17
D-glyceraldehyde 3-phosphate
in the absence of Co2+, at pH 7.5, 30C
0.0016
D-Xylulose 1-phosphate
-
-
0.095
dihydroxyacetone phosphate
in the absence of Co2+, at pH 7.5, 30C
0.0036
fructose 1,6-bisphosphate
-
50C, pH 7
0.009
fructose 1,6-bisphosphate
50C, pH 7
0.007
fructose 1-phosphate
-
chloroplastic enzyme
0.008
fructose 1-phosphate
-
cytoplasmic enzyme
0.0103
fructose 1-phosphate
-
chloroplastic enzyme
0.6
fructose 1-phosphate
-
chloroplastic enzyme
0.71
fructose 1-phosphate
-
50C, pH 7
0.8
fructose 1-phosphate
-
liver
1
fructose 1-phosphate
-
-
1
fructose 1-phosphate
-
cytosolic enzyme
1.1
fructose 1-phosphate
-
recombinant enzyme
1.4
fructose 1-phosphate
-
cytosolic enzyme
1.5
fructose 1-phosphate
-
-
1.6
fructose 1-phosphate
-
chloroplastic enzyme
1.6
fructose 1-phosphate
-
pH 5.5
1.7
fructose 1-phosphate
-
chloroplastic enzyme
1.7
fructose 1-phosphate
-
cytosolic enzyme
1.7
fructose 1-phosphate
-
chloroplastic enzyme
1.7
fructose 1-phosphate
-
mutant aldolase C Y363S
1.9
fructose 1-phosphate
-
pH 5.5
2
fructose 1-phosphate
-
-
2
fructose 1-phosphate
-
-
2.3
fructose 1-phosphate
-
cytosolic enzyme
2.3
fructose 1-phosphate
-
liver enzyme
2.9
fructose 1-phosphate
-
-
3
fructose 1-phosphate
-
-
3.7
fructose 1-phosphate
-
aldolase B
3.8
fructose 1-phosphate
-
pH 5.5
4.48
fructose 1-phosphate
50C, pH 7
5.3
fructose 1-phosphate
-
pH 7.6
6.1
fructose 1-phosphate
-
-
6.2
fructose 1-phosphate
-
pH 7.6
8.3
fructose 1-phosphate
-
recombinant non-muscle-type enzyme
9
fructose 1-phosphate
-
pH 9.2
9.3
fructose 1-phosphate
-
muscle-type enzyme
10
fructose 1-phosphate
-
muscle
10
fructose 1-phosphate
-
-
11
fructose 1-phosphate
-
non-muscle-type enzyme and recombinant muscle-type enzyme
11
fructose 1-phosphate
-
pH 9.3
11.3
fructose 1-phosphate
-
pH 7.6
18
fructose 1-phosphate
-
aldolase C
18
fructose 1-phosphate
-
pH 9.3
18.8
fructose 1-phosphate
-
-
25
fructose 1-phosphate
-
-
25
fructose 1-phosphate
-
aldolase C
27
fructose 1-phosphate
-
aldolase A
0.057
glyceraldehyde 3-phosphate
-
-
0.3
glyceraldehyde 3-phosphate
-
liver
1
glyceraldehyde 3-phosphate
-
muscle
0.065
glycerone phosphate
-
-
0.171
glycerone phosphate
pH 6.5, 70C
0.19
glycerone phosphate
pH 8.0, 48C, wild-type enzyme
0.34
glycerone phosphate
pH 8.0, 48C, mutant enzyme Y348F
0.4
glycerone phosphate
-
liver
1
glycerone phosphate
pH 7.6, 50C
2
glycerone phosphate
-
muscle
0.008
sedoheptulose 1,7-bisphosphate
-
pH 7.5, class II aldolase, recombinant enzyme
0.047
sedoheptulose 1,7-bisphosphate
-
pH 8, class I aldolase, recombinant enzyme
0.19
sedoheptulose 1,7-bisphosphate
in the absence of Co2+, at pH 7.5, 30C
0.006
sedoheptulose 1,7-diphosphate
-
-
10
sedoheptulose 1,7-diphosphate
-
-
0.0167
sedoheptulose 7-phosphate
-
pH 7.5, 30C
0.0195
sedoheptulose 7-phosphate
-
-
2
glycerone phosphate
pH 7.8, 55C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
Km-values of chimeric enzymes between two human aldolases A, B, or C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0002
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
turnover number less than 0.0002 sec-1, mutant enzyme K146A
0.001
D-fructose 1,6-bisphosphate
Escherichia coli
-
30C, N286D mutant
0.0019
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
mutant enzyme K146M
0.002
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
mutant enzyme D33S
0.0028
D-fructose 1,6-bisphosphate
Escherichia coli
-
30C, D109A mutant
0.003
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
mutant enzyme D33N
0.005
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
mutant enzyme E187Q
0.005
D-fructose 1,6-bisphosphate
Methylococcus capsulatus
Q602L6
in the absence of Co2+, at pH 7.5, 30C
0.011
D-fructose 1,6-bisphosphate
Homo sapiens
-
pH 7.4, 30C, enzyme from patients with intolerance
0.013
D-fructose 1,6-bisphosphate
Escherichia coli
-
E174A mutant, 30C
0.018
D-fructose 1,6-bisphosphate
Methylococcus capsulatus
Q602L6
in the presence of 0.02 mM Co2+, at substrate concentrations of 0.008-0.5 mM, at pH 7.5, 30C
0.026
D-fructose 1,6-bisphosphate
Sulfolobus tokodaii
F9VMT6
pH 8.0, 48C, mutant enzyme Y348F
0.027
D-fructose 1,6-bisphosphate
Sulfolobus tokodaii
F9VMT6
pH 8.0, 48C, wild-type enzyme
0.029
D-fructose 1,6-bisphosphate
Homo sapiens
-
pH 7.4, 10C, enzyme from patients with intolerance
0.03
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
E187Q mutant, pH 7.6, 22C
0.033
D-fructose 1,6-bisphosphate
Escherichia coli
-
E182A mutant, 30C
0.046
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
mutant enzyme E187A
0.055
D-fructose 1,6-bisphosphate
Methylococcus capsulatus
Q602L6
in the presence of 0.02 mM Co2+, at substrate concentrations of 0.5-1.5 mM, at pH 7.5, 30C
0.12
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
E187A mutant, pH 7.6, 22C
0.16
D-fructose 1,6-bisphosphate
Escherichia coli
-
N35A mutant, 30C
0.19
D-fructose 1,6-bisphosphate
Homo sapiens
-
pH 7.4, 10C, wild-type enzyme
0.19
D-fructose 1,6-bisphosphate
Homo sapiens
P05062
N334K mutant, 22C
0.19
D-fructose 1,6-bisphosphate
Escherichia coli
-
30C, N286A mutant
0.43
D-fructose 1,6-bisphosphate
Homo sapiens
P05062
W147R mutant, 22C
0.54
D-fructose 1,6-bisphosphate
Homo sapiens
P05062
L256P mutant, 22C
0.57
D-fructose 1,6-bisphosphate
Homo sapiens
P05062
Q354E mutant, 22C
0.58
D-fructose 1,6-bisphosphate
Escherichia coli
-
K325A mutant, 30C
0.61
D-fructose 1,6-bisphosphate
Homo sapiens
P05062
wild-type enzyme, 22C
0.63
D-fructose 1,6-bisphosphate
Giardia intestinalis
O97447
mutant enzyme D255A, in 50 mM K+-HEPES (pH 7.5), at 25C
0.65
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
mutant enzyme K107M
0.85
D-fructose 1,6-bisphosphate
Escherichia coli
-
S61A mutant, 30C
1.07
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
30C, AB_All mutant
1.53
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
30C, aldolase B
1.53
D-fructose 1,6-bisphosphate
Pseudomonas aeruginosa
-
in Tris-HCl pH 8.0, at 30C
1.6
D-fructose 1,6-bisphosphate
Bacillus methanolicus
I3EBM6
pH 7.8, 55C
1.63
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
pH 5.5
1.69
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
E189Q mutant, pH 7.6, 22C
2
D-fructose 1,6-bisphosphate
Escherichia coli
-
30C, D144A mutant
2.1
D-fructose 1,6-bisphosphate
Homo sapiens
-
pH 7.4, 30C, wild-type enzyme
2.1
D-fructose 1,6-bisphosphate
Neisseria meningitidis
-
at 30C in 50 mM Tris-HCl, 0.1 M potassium acetate buffer (pH 8.0)
2.2
D-fructose 1,6-bisphosphate
Escherichia coli
-
30C, D288A mutant
2.83
D-fructose 1,6-bisphosphate
Homo sapiens
-
mutant aldolase C Y363S
2.94
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
E189Q mutant, pH 7.6, 22C
2.94
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
30C, aldolase B
2.95
D-fructose 1,6-bisphosphate
Bacillus cereus
-
in Tris-HCl pH 8.0, at 30C
3.4
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
E189A mutant, pH 7.6, 22C
3.55
D-fructose 1,6-bisphosphate
Giardia intestinalis
-
at pH 7.5 and 25C, in the absence of Zn2+
3.55
D-fructose 1,6-bisphosphate
Giardia intestinalis
O97447
wild type enzyme, in 50 mM K+-HEPES (pH 7.5), at 25C
4.02
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
pH 9.3
4.7
D-fructose 1,6-bisphosphate
Homo sapiens
P04075
mutant enzyme G346S
5.03
D-fructose 1,6-bisphosphate
Trypanosoma brucei
-
pH 5.5
5.1
D-fructose 1,6-bisphosphate
Bacillus methanolicus
I3EBM6
pH 7.6, 50C
5.2
D-fructose 1,6-bisphosphate
Homo sapiens
-
-
5.28
D-fructose 1,6-bisphosphate
Trypanosoma brucei
-
pH 9.2
5.47
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
pH 7.6
5.8
D-fructose 1,6-bisphosphate
Escherichia coli
-
E181A mutant, 30C
6.08
D-fructose 1,6-bisphosphate
Escherichia coli
-
K325A mutant, 30C
6.08
D-fructose 1,6-bisphosphate
Homo sapiens
P05062
L256P mutant, 22C; Q354E mutant, 22C; wild-type enzyme, 22C
6.08
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
30C, AB_All mutant
6.3
D-fructose 1,6-bisphosphate
Escherichia coli
-
S61T mutant, 30C
7
D-fructose 1,6-bisphosphate
Escherichia coli
-
30C, D290A mutant
7.5
D-fructose 1,6-bisphosphate
Staphylococcus aureus
-
pH 9.3
7.87
D-fructose 1,6-bisphosphate
Staphylococcus aureus
-
pH 5.5
8.2
D-fructose 1,6-bisphosphate
Escherichia coli
-
30C, wild-type enzyme
8.2
D-fructose 1,6-bisphosphate
Leishmania mexicana
-
pH 7.6
8.5
D-fructose 1,6-bisphosphate
Escherichia coli
-
Q59A mutant, 30C
10.2
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
30C, aldolase A
10.2
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
at 30C
10.3
D-fructose 1,6-bisphosphate
Trypanosoma brucei
-
pH 7.6, native enzyme
10.5
D-fructose 1,6-bisphosphate
Escherichia coli
-
wild-type enzyme, 30C
10.7
D-fructose 1,6-bisphosphate
Homo sapiens
P04075
mutant enzyme E206K
10.9
D-fructose 1,6-bisphosphate
Trypanosoma brucei
-
pH 7.6, recombinant enzyme
12.3
D-fructose 1,6-bisphosphate
Escherichia coli
-
30C, D329A mutant
12.6
D-fructose 1,6-bisphosphate
Homo sapiens
-
aldolase C
13
D-fructose 1,6-bisphosphate
Edwardsiella ictaluri
-
30C
13.22
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
native wild type enzyme
13.9
D-fructose 1,6-bisphosphate
Staphylococcus aureus
-
pH 7.6
14
D-fructose 1,6-bisphosphate
Homo sapiens
-
wild-type and mutants, pH 7.4
14.2
D-fructose 1,6-bisphosphate
Escherichia coli
-
30C
15.8
D-fructose 1,6-bisphosphate
Lethenteron camtschaticum
-
non-muscle-type enzyme
16.5
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
30C, H156E mutant
16.7
D-fructose 1,6-bisphosphate
Homo sapiens
P04075
wild-type enzyme
16.76
D-fructose 1,6-bisphosphate
Staphylococcus carnosus
-
native enzyme, in Tris-HCl buffer (40 mM, pH 8.0), at 25C
17.9
D-fructose 1,6-bisphosphate
Lethenteron camtschaticum
-
recombinant non-muscle-type enzyme
20.1
D-fructose 1,6-bisphosphate
Homo sapiens
-
aldolase B
20.3
D-fructose 1,6-bisphosphate
Staphylococcus carnosus
-
recombinant fusion protein DLF, in Tris-HCl buffer (40 mM, pH 8.0), at 25C
21
D-fructose 1,6-bisphosphate
Mycobacterium tuberculosis
P9WQA3
pH 7.3, 28C
30.1
D-fructose 1,6-bisphosphate
Mycobacterium tuberculosis
-
in Tris-HCl pH 8.0, at 30C
33
D-fructose 1,6-bisphosphate
Rattus norvegicus
-
aldolase C
36.9
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
E189A mutant, pH 7.6, 22C
40
D-fructose 1,6-bisphosphate
Vigna radiata
-
pH 7.5, 30C
42.2
D-fructose 1,6-bisphosphate
Oryctolagus cuniculus
-
native recombinant enzyme, pH 7.6, 22C
45.7
D-fructose 1,6-bisphosphate
Magnaporthe grisea
-
in Tris-HCl pH 8.0, at 30C
45.9
D-fructose 1,6-bisphosphate
Gallus gallus
-
-
46
D-fructose 1,6-bisphosphate
Magnaporthe grisea
-
at pH 7.8
46.1
D-fructose 1,6-bisphosphate
Lethenteron camtschaticum
-
muscle-type enzyme
49.3
D-fructose 1,6-bisphosphate
Lethenteron camtschaticum
-
recombinant muscle-type enzyme
59.7
D-fructose 1,6-bisphosphate
Homo sapiens
-
aldolase A
64.5
D-fructose 1,6-bisphosphate
Daucus carota
-
-
0.008
D-Fructose 1-phosphate
Homo sapiens
-
pH 7.4, 30C, enzyme from patients with intolerance
0.019
D-Fructose 1-phosphate
Homo sapiens
-
pH 7.4, 10C, enzyme from patients with intolerance
0.059
D-Fructose 1-phosphate
Homo sapiens
P05062
Q354E mutant, 22C
0.085
D-Fructose 1-phosphate
Homo sapiens
P05062
N334K mutant, 22C
0.12
D-Fructose 1-phosphate
Homo sapiens
-
pH 7.4, 10C, wild-type enzyme
0.25
D-Fructose 1-phosphate
Homo sapiens
P05062
W147R mutant, 22C
0.38
D-Fructose 1-phosphate
Homo sapiens
P05062
L256P mutant, 22C
0.63
D-Fructose 1-phosphate
Oryctolagus cuniculus
-
30C, aldolase A
0.63
D-Fructose 1-phosphate
Oryctolagus cuniculus
-
at 30C
0.67
D-Fructose 1-phosphate
Homo sapiens
P05062
wild-type enzyme, 22C
1.47
D-Fructose 1-phosphate
Oryctolagus cuniculus
-
30C, AB_All mutant
2
D-Fructose 1-phosphate
Homo sapiens
-
pH 7.4, 30C, wild-type enzyme
2.8
D-Fructose 1-phosphate
Homo sapiens
-
-
6.08
D-Fructose 1-phosphate
Homo sapiens
P05062
wild-type enzyme, 22C
6.08
D-Fructose 1-phosphate
Oryctolagus cuniculus
-
30C, AB_All mutant; 30C, aldolase A; 30C, aldolase B
0.01
D-fructose-1,6-bisphosphate
Mycobacterium tuberculosis
-
mutant E169A, pH 7.8, 22C
0.11
D-fructose-1,6-bisphosphate
Mycobacterium tuberculosis
-
mutant G167A/G166A, pH 7.8, 22C
0.17
D-fructose-1,6-bisphosphate
Mycobacterium tuberculosis
-
mutant G167A, pH 7.8, 22C
0.45
D-fructose-1,6-bisphosphate
Mycobacterium tuberculosis
-
mutant D276A, pH 7.8, 22C
2.67
D-fructose-1,6-bisphosphate
Mycobacterium tuberculosis
-
mutant E168A, pH 7.8, 22C
12
D-fructose-1,6-bisphosphate
Mycobacterium tuberculosis
-
wild-type, pH 7.8, 22C
0.002
D-glyceraldehyde 3-phosphate
Methylococcus capsulatus
Q602L6
in the absence of Co2+, at pH 7.5, 30C
0.1
D-glyceraldehyde 3-phosphate
Sulfolobus tokodaii
F9VMT6
pH 8.0, 48C, mutant enzyme Y348F
0.56
D-glyceraldehyde 3-phosphate
Bacillus methanolicus
I3EBM6
pH 7.6, 50C
0.91
D-glyceraldehyde 3-phosphate
Sulfolobus tokodaii
F9VMT6
pH 8.0, 48C, wild-type enzyme
12.6
D-glyceraldehyde 3-phosphate
Bacillus methanolicus
I3EBM6
pH 7.8, 55C
0.002
dihydroxyacetone phosphate
Methylococcus capsulatus
Q602L6
in the absence of Co2+, at pH 7.5, 30C
0.167
fructose 1-phosphate
Oryctolagus cuniculus
-
pH 9.3
0.183
fructose 1-phosphate
Oryctolagus cuniculus
-
pH 5.5
0.267
fructose 1-phosphate
Oryctolagus cuniculus
-
pH 7.6
0.45
fructose 1-phosphate
Staphylococcus aureus
-
pH 5.5
0.583
fructose 1-phosphate
Staphylococcus aureus
-
pH 9.3
0.75
fructose 1-phosphate
Homo sapiens
-
mutant aldolase C Y363S
1.05
fructose 1-phosphate
Staphylococcus aureus
-
pH 7.6
1.13
fructose 1-phosphate
Trypanosoma brucei
-
pH 5.5
1.27
fructose 1-phosphate
Trypanosoma brucei
-
pH 9.2
1.28
fructose 1-phosphate
Homo sapiens
-
aldolase A
1.38
fructose 1-phosphate
Lethenteron camtschaticum
-
muscle-type enzyme
1.48
fructose 1-phosphate
Homo sapiens
-
aldolase C
1.55
fructose 1-phosphate
Lethenteron camtschaticum
-
recombinant muscle-type enzyme
1.7
fructose 1-phosphate
Trypanosoma brucei
-
pH 7.6
2.67
fructose 1-phosphate
Rattus norvegicus
-
aldolase C
3.6
fructose 1-phosphate
Lethenteron camtschaticum
-
non-muscle-type enzyme
3.65
fructose 1-phosphate
Lethenteron camtschaticum
-
recombinant non-muscle-type enzyme
10.8
fructose 1-phosphate
Homo sapiens
-
aldolase B
0.1
glycerone phosphate
Sulfolobus tokodaii
F9VMT6
pH 8.0, 48C, mutant enzyme Y348F
0.4
glycerone phosphate
Bacillus methanolicus
I3EBM6
pH 7.6, 50C
0.91
glycerone phosphate
Sulfolobus tokodaii
F9VMT6
pH 8.0, 48C, wild-type enzyme
0.003
sedoheptulose 1,7-bisphosphate
Methylococcus capsulatus
Q602L6
in the absence of Co2+, at pH 7.5, 30C
25.2
sedoheptulose 1,7-diphosphate
Daucus carota
-
-
33.3
sedoheptulose 7-phosphate
Vigna radiata
-
pH 7.5, 30C
8
glycerone phosphate
Bacillus methanolicus
I3EBM6
pH 7.8, 55C
additional information
additional information
Synechococcus elongatus PCC 7942
-
-
-
additional information
additional information
Oryctolagus cuniculus
-
turnover-numbers of wild-type and mutant enzymes
-
additional information
additional information
Cavia porcellus
-
Km for fructose 1,6-diphosphate is dependent on the protein concentration in the range 0.01-0.05 mM
-
additional information
additional information
Homo sapiens
-
turnover-numbers of chimeric enzymes between two human aldolases A, B, or C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.066
D-fructose 1,6-bisphosphate
Bacillus cereus
-
in Tris-HCl pH 8.0, at 30C
106
0.44
D-fructose 1,6-bisphosphate
Pseudomonas aeruginosa
-
in Tris-HCl pH 8.0, at 30C
106
0.8
D-fructose 1,6-bisphosphate
Bacillus methanolicus
I3EBM6
pH 7.8, 55C
106
9
D-fructose 1,6-bisphosphate
Magnaporthe grisea
-
in Tris-HCl pH 8.0, at 30C
106
10.8
D-fructose 1,6-bisphosphate
Mycobacterium tuberculosis
-
in Tris-HCl pH 8.0, at 30C
106
31.3
D-fructose 1,6-bisphosphate
Bacillus methanolicus
I3EBM6
pH 7.6, 50C
106
40
D-fructose 1,6-bisphosphate
Giardia intestinalis
O97447
mutant enzyme D255A, in 50 mM K+-HEPES (pH 7.5), at 25C
106
1080
D-fructose 1,6-bisphosphate
Staphylococcus carnosus
-
recombinant fusion protein DLF, in Tris-HCl buffer (40 mM, pH 8.0), at 25C
106
1160
D-fructose 1,6-bisphosphate
Staphylococcus carnosus
-
native enzyme, in Tris-HCl buffer (40 mM, pH 8.0), at 25C
106
2000
D-fructose 1,6-bisphosphate
Giardia intestinalis
O97447
wild type enzyme, in 50 mM K+-HEPES (pH 7.5), at 25C
106
0.28
D-fructose-1,6-bisphosphate
Mycobacterium tuberculosis
-
mutant E169A, pH 7.8, 22C
1895
2.5
D-fructose-1,6-bisphosphate
Mycobacterium tuberculosis
-
mutant D276A, pH 7.8, 22C
1895
5.33
D-fructose-1,6-bisphosphate
Mycobacterium tuberculosis
-
mutant G167A/G166A, pH 7.8, 22C
1895
8
D-fructose-1,6-bisphosphate
Mycobacterium tuberculosis
-
mutant G167A, pH 7.8, 22C
1895
88.33
D-fructose-1,6-bisphosphate
Mycobacterium tuberculosis
-
mutant E168A, pH 7.8, 22C
1895
300
D-fructose-1,6-bisphosphate
Mycobacterium tuberculosis
-
wild-type, pH 7.8, 22C
1895
0.29
D-glyceraldehyde 3-phosphate
Sulfolobus tokodaii
F9VMT6
pH 8.0, 48C, mutant enzyme Y348F
147
1.4
D-glyceraldehyde 3-phosphate
Bacillus methanolicus
I3EBM6
pH 7.6, 50C
147
4.7
D-glyceraldehyde 3-phosphate
Sulfolobus tokodaii
F9VMT6
pH 8.0, 48C, wild-type enzyme
147
50.4
D-glyceraldehyde 3-phosphate
Bacillus methanolicus
I3EBM6
pH 7.8, 55C
147
0.29
glycerone phosphate
Sulfolobus tokodaii
F9VMT6
pH 8.0, 48C, mutant enzyme Y348F
482
0.4
glycerone phosphate
Bacillus methanolicus
I3EBM6
pH 7.6, 50C
482
4
glycerone phosphate
Bacillus methanolicus
I3EBM6
pH 7.8, 55C
482
4.7
glycerone phosphate
Sulfolobus tokodaii
F9VMT6
pH 8.0, 48C, wild-type enzyme
482
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.11
([3-hydroxy-2-oxo-4-[(phosphonomethoxy)methyl]pyridin-1(2H)-yl]methyl)phosphonic acid
-
at pH 7.5 and 25C
0.014
([3-hydroxy-2-oxo-4-[2-(phosphonooxy)ethyl]pyridin-1(2H)-yl]methyl)phosphonic acid
-
at pH 7.5 and 25C
0.09
([3-hydroxy-4-[(1R)-1-hydroxy-2-(phosphonooxy)ethyl]-2-oxopyridin-1(2H)-yl]methyl)phosphonic acid
-
at pH 7.5 and 25C
0.01
([3-hydroxy-4-[(1S)-1-hydroxy-2-(phosphonooxy)ethyl]-2-oxopyridin-1(2H)-yl]methyl)phosphonic acid
-
at pH 7.5 and 25C
0.015
([4,5-dihydroxy-6-[2-(phosphonooxy)ethyl]pyridin-3-yl]methyl)phosphonic acid
-
at pH 7.5 and 25C
0.125
1-hydroxy-2-naphthaldehyde 6-phosphate
-
wild-type enzyme
0.9
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl dihydrogen phosphate
-
at pH 7.5 and 25C
0.000234
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.00031
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.0008
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.004
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.067
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
2.3
2-hydroxy-2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl dihydrogen phosphate
-
at pH 7.5 and 25C
0.1
2-oxo-2-[(phenylsulfonyl)amino]ethyl phosphate
-
-
0.35
2-[(methylsulfonyl)amino]-2-oxoethyl phosphate
-
-
0.00067
2-[(trihydroxyphosphoranyl)oxy]acetohydrazide
-
-
0.37
2-[(trihydroxyphosphoranyl)oxy]acetohydrazide
-
-
0.00017
2-[hydroxy(3-hydroxypropyl)amino]-2-oxoethyl dihydrogen phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.000416
2-[hydroxy(3-hydroxypropyl)amino]-2-oxoethyl dihydrogen phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.0047
2-[hydroxy(3-hydroxypropyl)amino]-2-oxoethyl dihydrogen phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
2.5
2-[hydroxy(3-hydroxypropyl)amino]-2-oxoethyl dihydrogen phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.000185
2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.000195
2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.0003
2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.0055
2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.4
2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.000013
3-[hydroxy[(phosphonooxy)acetyl]amino]propyl dihydrogen phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.0002
3-[hydroxy[(phosphonooxy)acetyl]amino]propyl dihydrogen phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.264
3-[hydroxy[(phosphonooxy)acetyl]amino]propyl dihydrogen phosphate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.00012
4-[hydroxy[(phosphonooxy)acetyl]amino]butyl hexanoate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.000195
4-[hydroxy[(phosphonooxy)acetyl]amino]butyl hexanoate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.00028
4-[hydroxy[(phosphonooxy)acetyl]amino]butyl hexanoate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.001
4-[hydroxy[(phosphonooxy)acetyl]amino]butyl hexanoate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.85
4-[hydroxy[(phosphonooxy)acetyl]amino]butyl hexanoate
-
in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.1824
5-chloro-8-hydroxyquinoline
-
native-rMtFBA, Ki = 182.4 microM and KI = 219.5 microM
0.1934
5-chloro-8-hydroxyquinoline
-
C-His-rMtFBA, Ki = 193.4 microM and KI = 220.9 microM. This indicates a possible use of C-His-rMtFBA for screening of MtFBA inhibitors
0.0233
5-formyl-6-hydroxynaphthalen-2-yl dihydrogen phosphate
-
-
3.1
ADP
-
pH 7.5, 30C
7.5
AMP
-
pH 7.5, 30C
0.38
D-erythrose 4-phosphate
-
-
2 - 5
D-fructose 1,6-bisphosphate
pH 7.8, 55C
22
D-fructose 1,6-bisphosphate
pH 7.6, 50C
0.06
D-glucitol 1,6-bisphosphate
-
-
0.1
D-glucitol 1,6-bisphosphate
-
-
0.17
D-glucitol 1,6-bisphosphate
-
-
0.0073
D-mannitol 1,6-bisphosphate
-
-
0.073
D-mannitol 1,6-bisphosphate
-
-
0.4
D-mannitol 1,6-bisphosphate
-
-
0.12
D-ribulose 1,5-bisphosphate
-
pH 7.5, class II aldolase, purified enzyme
0.37
D-ribulose 1,5-bisphosphate
-
pH 8, class I aldolase, recombinant enzyme
0.59
D-ribulose 1,5-bisphosphate
-
pH 7.5, class II aldolase, recombinant enzyme
0.13
dihydroxyacetone phosphate
-
30C, wild-type enzyme
0.238
dihydroxyacetone phosphate
-
wild-type, pH 7.8, 22C
1.7
dihydroxyacetone phosphate
-
30C, N268A mutant
0.045
hexitol-1,6-bisphosphate
-
-
0.0033
N'-hydroxy-2-[(trihydroxyphosphoranyl)oxy]ethanimidamide
-
-
0.001
N-hydroxy-2-[(trihydroxyphosphoranyl)oxy]acetamide
-
-
0.028
naphthalene-2,6-bisphosphate
-
-
0.00028
naphthyl 2,6-bisphosphate
-
wild-type enzyme
0.013
naphthyl 2,6-bisphosphate
-
mutant enzyme K107M
0.00023
phosphate
-
pH 7.3, 5C
0.00118
phosphate
-
pH 7.3, 37C
0.00001
phosphoglycolo hydroxamic acid
-
-
0.00001
phosphoglycolo hydroxamic acid
-
-
0.001
phosphoglycolo hydroxamic acid
-
-
0.0023
phosphoglycolo-amidoxime
-
-
0.00034
phosphoglycolo-hydrazide
-
-
0.0024
Phosphoglycolohydroxamate
-
at pH 7.5 and 25C, in the absence of Zn2+
2.2
ribose 5-phosphate
-
pH 7.5, 30C
0.001
tagatose 1,6-bisphosphate
-
at pH 7.5 and 25C
1.2
[(3-hydroxy-2-oxopyridin-1(2H)-yl)methyl]phosphonic acid
-
at pH 7.5 and 25C
0.81
[2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl]phosphonic acid
-
at pH 7.5 and 25C
0.97
[[(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)methoxy]methyl]phosphonic acid
-
at pH 7.5 and 25C
0.8
[[3-hydroxy-2-oxo-4-(2-phosphonoethyl)pyridin-1(2H)-yl]methyl]phosphonic acid
-
at pH 7.5 and 25C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.057
2-carboxy-6-(phosphonomethyl)pyridinium chloride
Mycobacterium tuberculosis
-
pH 7.3, 28C
0.078
2-carboxy-6-(phosphonomethyl)pyridinium chloride
Bacillus cereus
-
pH 7.3, 28C
0.095
2-carboxy-6-(phosphonomethyl)pyridinium chloride
Magnaporthe grisea
-
pH 7.3, 28C
0.13
2-carboxy-6-(phosphonomethyl)pyridinium chloride
Pseudomonas aeruginosa
-
pH 7.3, 28C
0.33
5-chloro-8-hydroxyquinoline
Mycobacterium tuberculosis
-
NADH-linked enzymatic assay
0.533
5-chloro-8-hydroxyquinoline
Mycobacterium tuberculosis
-
determined by the colorimetric assay
0.02
5-formyl-6-hydroxynaphthalen-2-yl dihydrogen phosphate
Trypanosoma brucei
-
15 min incubation time
0.496
8-hydroxyquinoline
Mycobacterium tuberculosis
-
NADH-linked enzymatic assay
0.5
8-hydroxyquinoline
Mycobacterium tuberculosis
-
determined by the colorimetric assay
0.028
dipicolinic acid
Mycobacterium tuberculosis
-
pH 7.3, 28C
0.079
dipicolinic acid
Magnaporthe grisea
-
pH 7.3, 28C
0.095
dipicolinic acid
Pseudomonas aeruginosa
-
pH 7.3, 28C
0.15
dipicolinic acid
Bacillus cereus
-
pH 7.3, 28C
0.008
EDTA
Bacillus cereus
-
pH 7.3, 28C
0.041
EDTA
Pseudomonas aeruginosa
-
pH 7.3, 28C
0.048
EDTA
Mycobacterium tuberculosis
-
pH 7.3, 28C
0.053
EDTA
Magnaporthe grisea
-
pH 7.3, 28C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
-
substrate: D-fructose 1,6-bisphosphate, 50C, pH not specified in the publication, enzyme from starch-grown cells
0.044
-
pH not specified in the publication, 37C, activity in undialyzed cell extracts
0.123
-
after 1fold purification, at 25C
0.13
N334K mutant, D-fructose 1-phosphate as substrate
0.28
N334K mutant, D-fructose 1,6-bisphosphate as substrate
0.3
-
-
0.38
W147R mutant, D-fructose 1-phosphate as substrate
0.58
L256P mutant, D-fructose 1-phosphate as substrate
0.64
W147R mutant, D-fructose 1,6-bisphosphate as substrate
0.81
L256P mutant, D-fructose 1,6-bisphosphate as substrate
0.86
Q354E mutant, D-fructose 1,6-bisphosphate as substrate
0.88
Q354E mutant, D-fructose 1-phosphate as substrate
0.94
wild-type enzyme, D-fructose 1-phosphate as substrate
0.97
wild-type enzyme, D-fructose 1,6-bisphosphate as substrate
2.8
-
pH 7.5, 37C
3.2
-
enzyme form I
4.8
-
enzyme form II
5.3
-
strain 168, spore
5.92
-
muscle-type enzyme
6.1
mutant enzyme G346S
6.4
-
-
7.01
-
recombinant non-muscle-type enzyme
7.18
-
cytosolic enzyme
7.77
-
class II aldolase
7.8
-
chloroplastic enzyme
8
-
A4 isoenzyme
8.62
-
class I aldolase
8.85
-
strain PCI 219, vegetative cell
10.7
-
-
10.7
-
after 87fold purification, at 25C
11.5
-
crude cell extract, at 30C
11.7
-
A2C2 isoenzyme
11.8
-
A1C3 isoenzyme
12.2
-
synthesis D-glyceraldehyde-3-phosphate + dihydroxyacetone phosphate; synthesis propanal + dihydroxyacetone phosphate
12.3
-
A3C1 isoenzyme
13
-
A4 isoenzyme
13.2
-
strain 168, vegetative cell
14.8
-
-
15.7
mutant enzyme E206K
17.27
-
liver enzyme
18.5
-
recombinat muscle-type enzyme
20
-
class I aldolase
22
-
class II aldolase
22.3
wild-type enzyme
22.8
-
pH 7.2, 25C
25.5
-
-
26.7
-
splitting of fructose 1,6-bisphosphate
32.3
-
strain PCI 219, spore
34.85
-
purified native-rMtFBA
35.05
-
purified C-His-rMtFBA
38.4
-
pH 7.5, 37C
70.3
-
after 6.1fold purification, at 30C
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
-
6
-
E187A and E189Q mutant
6 - 8.5
-
class I aldolase
6.5 - 8.5
-
with D-fructose 1,6-bisphosphate as substrate
6.5 - 9
-
aldolase I
6.8 - 7
-
-
7
-
cleavage of fructose 1-phosphate
7 - 7.5
-
class II aldolase
7 - 8
-
broad pH optimum in glycylglycine buffer and imidazole buffer
7.3
-
soluble enzyme
7.4
-
cleavage of D-fructose 1,6-bisphosphate
7.4 - 7.8
-
-
7.5
-
with fructose 1-phosphate as substrate
7.5
-
immobilized enzyme
7.5
-
in Tris-HCl buffer
8
-
broad, plastidic and cytosolic enzyme
8
-
broad optimum, wild-type and E189A mutant
8.5 - 9.5
-
-
8.6
-
aldolase class II
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 12
-
pH 4: about 80% of maximal activity, pH 12: about 75% of maximal activity
5.5 - 9
-
pH 5.5: about 40% of maximal activity, pH 9.0: about 30% of maximal activity
5.5 - 9
-
pH 5.5: about 25% of maximal activity, pH 9.0: about 75% of maximal activity
5.5 - 9.1
-
pH 5.5: 58% of maximal activity, pH 9.1: 85% of maximal activity
5.5 - 9.3
-
more than 50% of optimal activity in the range, recombinant enzyme
6 - 9
-
pH 6.0: about 75% of maximal activity, pH 9.0: about 70% of maximal activity, immobilized enzyme; pH 6.0: about 85% of maximal activity, pH 9.0: about 60% of maximal activity, soluble enzyme
6 - 9.5
-
about 30% of maximal activity at pH 6.0 and at pH 9.5, D-fructose 1,6-bisphosphate cleavage
6.3 - 9.5
-
pH 6.3: about 10% of maximal activity, pH 9.5: about 85% of maximal activity
6.7 - 8.5
-
pH 6.7: 50% of maximal activity, pH 8.5: about 50% of maximal activity
6.8 - 8.8
-
pH 6.8: about 45% of maximal activity, pH 8.8: about 25% of maximal activity
7 - 10
-
about 25% of maximal activity at pH 7.0 and pH 10.0
7.3 - 8.5
pH 7.3: about 70% of maximal activity, pH 8.5: about 55% of maximal activity
7.5
-
steep drop in activity above
7.7 - 9.3
-
pH 7.7: about 40% of maximal activity, pH 9.3: about 95% of maximal activity
8 - 9
-
pH 8.0: about 60% of maximal activity, pH 9.0: about 10% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
soluble enzyme
45
-
immobilized enzyme
50
-
assay at
50
-
assay at, temperature optimum for the specific acitivity of MJ0400-His6
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
-
gradual loss of activity above, enzyme from patients with fructose intolerance
25 - 50
-
25C: about 90% of maximal activity, 50C: about 50% of maximal activity, immobilized enzyme; 25C: about 95% of maximal activity, 50C: about 50% of maximal activity, soluble enzyme
25 - 60
-
about 40% of maximal activity at 25C and 60C
30 - 55
-
30C: about 65% of maximal activity, 55C: about 40% of maximal activity
32 - 43
-
32C: about 30% of maximal activity, 43C: about 10% of maximal activity
40
-
wild-type enzyme, activity is stable up to 40C, declines sharply above 40C
60
little activity below
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
isoelectric focusing, pH gradient pH 3.5 - pH 10
5.6
-
native-rMtFBA, agreeing with the calculation from their sequence, 5.42
5.9
-
C-His-rMtFBA, agreeing with the calculation from their sequence, 5.82
7
-
neutral or slightly acidic pI, isoelectric focussing, pH gradient 4.5-9
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
basal lamina surrounding the body cavity
Manually annotated by BRENDA team
-
isoenzyme III, IV, and V
Manually annotated by BRENDA team
Archaeoglobus fulgidus 7324
-
-
-
Manually annotated by BRENDA team
channels connecting the esophagus to the cuticle, basal lamina surrounding the esophagus
Manually annotated by BRENDA team
-
aldolase A is localized in limb and collecting ducts of the medulla and in the distal tubules and glomerula of the cortex; aldolase B is localized in proximal cells
Manually annotated by BRENDA team
-
etiolated leaves contain 2 isoenzymes
Manually annotated by BRENDA team
-
tail muscle
Manually annotated by BRENDA team
-
flexor digitorum brevis
Manually annotated by BRENDA team
Leishmania donovani 2S
-
-
-
Manually annotated by BRENDA team
-
storage root
Manually annotated by BRENDA team
-
of seedling, especially in the apical region. Aldolase physically associates with vacuolar H+-ATPase in roots
Manually annotated by BRENDA team
FBA is more strongly expressed in roots than in leaves and stems
Manually annotated by BRENDA team
-
germinating
Manually annotated by BRENDA team
-
endosperm
Manually annotated by BRENDA team
-
germinated
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
acidic isoenzyme
Manually annotated by BRENDA team
-
heat inducible enzyme, adhered to the chloroplast membrane
Manually annotated by BRENDA team
-
non-heat inducible enzyme
Manually annotated by BRENDA team
-
basic isoenzyme
Manually annotated by BRENDA team
-
class II aldolase
Manually annotated by BRENDA team
Leishmania donovani 2S
-
-
-
Manually annotated by BRENDA team
-
strong ALDOA expression is observed along the ruffling membrane and lamellipodia, and it is colocalized with the actin cytoskeleton in lamellipodia
Manually annotated by BRENDA team
-
both chloroplastic and cytosolic phosphofructoaldolase isozymes are present in the pea leaf nucleus
Manually annotated by BRENDA team
-
class I aldolase
Manually annotated by BRENDA team
additional information
-
HIP 44 is not present in root or coleoptile plastids
-
Manually annotated by BRENDA team
additional information
-
FBPasealdolase complex is located on an actinin of the Z-line. The stability of the complex is regulated by calcium ions. Elevated calcium concentration decreases association constant of FBPasealdolase and FBPase-alpha-actinin complex, causes fast dissociation of FBPase from the Z-line and slow accumulation of aldolase within the I-band and M-line. Release of Ca2+ during muscle contraction might result, simultaneously, in the inhibition of glyconeogenesis and in the acceleration of glycolysis
-
Manually annotated by BRENDA team
additional information
-
probably specific subcellular location regulated by calpain-3, calpain-3 necessary for proper localization; triad
-
Manually annotated by BRENDA team