Information on EC 4.1.2.13 - fructose-bisphosphate aldolase

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

EC NUMBER
COMMENTARY
4.1.2.13
-
RECOMMENDED NAME
GeneOntology No.
fructose-bisphosphate aldolase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
condensation
-
-
-
-
elimination
-
-
of an aldehyde, C-C bond cleavage
-
PATHWAY
KEGG Link
MetaCyc Link
1,3-propanediol biosynthesis (engineered)
-
Biosynthesis of secondary metabolites
-
Calvin-Benson-Bassham cycle
-
Carbon fixation in photosynthetic organisms
-
formaldehyde assimilation II (RuMP Cycle)
-
formaldehyde assimilation III (dihydroxyacetone cycle)
-
Fructose and mannose metabolism
-
gluconeogenesis I
-
gluconeogenesis II (Methanobacterium thermoautotrophicum)
-
gluconeogenesis III
-
Glycolysis / Gluconeogenesis
-
glycolysis I (from glucose-6P)
-
glycolysis II (from fructose-6P)
-
glycolysis III (from glucose)
-
glycolysis IV (plant cytosol)
-
glycolysis V (Pyrococcus)
-
glycolysis VI (metazoan)
-
Metabolic pathways
-
Methane metabolism
-
Microbial metabolism in diverse environments
-
Pentose phosphate pathway
-
sucrose biosynthesis I (from photosynthesis)
-
sucrose degradation V (sucrose alpha-glucosidase)
-
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 ACCESSION NO.
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 Fba
P00883
-
class I fructose 1,6-bisphosphate aldolase
-
-
class I fructose bisphosphate aldolase
P00883
-
class I muscle fructose bis-phosphate aldolase
P00883
-
class II aldolase
P56109
-
class II aldolase
P14540
-
class II FBP aldolase
P67475
-
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
P56109
-
class II fructose bisphosphate aldolase
P67475
-
class II fructose bisphosphate aldolase
P14540
-
class II fructose-1,6-bisphosphate aldolase
P67475
-
class IIa fructose 1,6-bisphosphate aldolase
P67475
-
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
Q602L6
the Methylococcus capsulatus enzyme belongs to the type B of class II fructose-1,6-bisphosphate aldolases
FBP aldolase
-
-
-
-
FBP aldolase
A1YZ23
-
FBP aldolase
Anoxybacillus gonensis G2
A1YZ23
-
-
FBP aldolase
-
-
FBP aldolase
-
-
-
FBP aldolase
-
-
FBP aldolase
-
-
FBP aldolase
-
-
FBP aldolase
-
-
FBP aldolase/phosphatase
F9VMT6
bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13
FBP aldolase/phosphatase
Sulfolobus tokodaii 7
F9VMT6
bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13
-
FBP aldolase/phosphatase
-
-
FBPA
Schistosoma japonicum Formosan
Q1HDV3
-
-
FBPA
Staphylococcus carnosus CECT 4491
-
-
-
FBPA/P
F9VMT6
bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13
FBPA/P
Sulfolobus tokodaii 7
F9VMT6
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
P53442
-
Fructose 1,6-bisphosphate aldolase
-
-
-
-
Fructose 1,6-bisphosphate aldolase
-
-
Fructose 1,6-bisphosphate aldolase
-
-
Fructose 1,6-bisphosphate aldolase
Q55664
-
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
P56109
-
fructose bis-phosphate aldolase
P00883
-
fructose bis-phosphate aldolase
P14540
-
Fructose bisphosphate aldolase
-
-
-
-
Fructose bisphosphate aldolase
-
-
Fructose bisphosphate aldolase
P53449
-
Fructose bisphosphate aldolase
-
-
Fructose bisphosphate aldolase
P16096
-
Fructose bisphosphate aldolase
-
-
Fructose bisphosphate aldolase
C1J959
-
Fructose diphosphate aldolase
-
-
-
-
fructose-1,6-biphosphate aldolase
-
-
fructose-1,6-bisphosphate aldolase
O97447
-
fructose-1,6-bisphosphate aldolase
-
-
fructose-1,6-bisphosphate aldolase
-
-
fructose-1,6-bisphosphate aldolase
Q602L6
-
fructose-1,6-bisphosphate aldolase
-
-
fructose-1,6-bisphosphate aldolase
Q1HDV2
-
fructose-1,6-bisphosphate aldolase
Q1HDV3
-
fructose-1,6-bisphosphate aldolase
Schistosoma japonicum Formosan
Q1HDV3
-
-
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
P00883
-
fructose-1,6-bisphosphate aldolase/phosphatase
F9VMT6
bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13
fructose-1,6-bisphosphate aldolase/phosphatase
Sulfolobus tokodaii 7
F9VMT6
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
-
-
-
-
Muscle-type aldolase
-
-
-
-
Ov-fba-1
Q9U9R9
-
Phosphofructoaldolase
-
-
-
-
SMALDO
-
-
-
-
SSO0286
Q980K6
locus name
SSO0286
Q980K6
locus name
-
STK_03180
F9VMT6
locus name. The bifunctional enzyme also shows activity of EC 3.1.3.11
STK_03180
Sulfolobus tokodaii 7
F9VMT6
locus name. The bifunctional enzyme also shows activity of EC 3.1.3.11
-
Zymohexase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-52-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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
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
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
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 ACCESSION NO.
COMMENTARY
LITERATURE
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
Q980K6
gluconeogenic pathway
physiological function
Archaeoglobus fulgidus 7324
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
physiological function
-
gluconeogenic pathway
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
Q9RHA2
-
-
-
-
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
P0AB71
-
-
-
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
P04075
-
-
-
?
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
-
-
-
-
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
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
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
Q703I2, -
-
-
-
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
-, 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
-
-
-
-
?
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
-, P67475
-
-
-
?
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
A1YZ23, -
-
-
-
?
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
P56109
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
B5B3T4, -
-
-
-
?
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
O97447
-
-
-
?
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
P58314, -
preferred substrate, reaction intermediate is Schiff base
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
P58315, -
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
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
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
A1YZ23
-
-
-
?
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
-, Q602L6
-
-
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
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
-
-
-
-
-
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
P05062
-
-
?
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
P58314, -
-
-
?
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
P58315, -
-
-
?
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
Peptoniphilus asaccharolyticus 228
-
-
-
-
-
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
P67475
-
-
-
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
P14540
-
-
-
-
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
Q703I2, -
-
-
-
?
D-Xylulose 1-phosphate
?
show the reaction diagram
-
110% of the activity with fructose 1,6-diphosphate
-
-
-
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
-, Q602L6
-
-
-
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
-
-
-
-
-
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
Q980K6
-
-
-
?
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
Sulfolobus tokodaii, Sulfolobus tokodaii 7
F9VMT6
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
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
-, Q602L6
-
-
-
?
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
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
Q980K6
-
-
-
?
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
-
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
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
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
P67475
-
-
-
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
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 ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activates
Ca2+
A1YZ23, -
1 mM, 82% increase of activity
Cd2+
-
can partially restore activity of metal depleted enzyme
Cd2+
-, Q602L6
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+
Q9RHA2
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+
Q703I2, -
-
Co2+
A1YZ23, -
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+
-, Q602L6
the enzyme activity increases 2.5times in the presence of Co2+
Cu2+
-
stimulates
Cu2+
-
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Cu2+
-, Q602L6
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
Fe3+
-
maximal activity only when both 8 mM Cys and 0.1 mM Fe2+ are present. Fe3+ or Mn2+ can replace Fe2+
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+
A1YZ23, -
1 mM, 30% increase of activity
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+
F9VMT6
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+
Na+
-
stimulates
Na+
-
enhances activity of aldolase II
NH4+
Anacystis sp., Clostridium sp.
-
stimulates
NH4+
-
stimulates
NH4+
-
stimulates
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+
Q9RHA2
can replace Co2+ at a limited rate
Zn2+
P67475
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+
A1YZ23, -
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+
O97447
FBPA belongs to the class II zinc-dependent aldolase family, each subunit contains a Zn2+ cofactor
Zn2+
-
dependent
Zn2+
-, Q602L6
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
Mn2+
-
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of 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
A1YZ23, -
Cd2+ has no effect on activity
additional information
-, Q602L6
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 ACCESSION NO.
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-hydroxy-2-naphthaldehyde 6-phosphate
-
slow-binding
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-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-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
-
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
Agaricic acid
-
50% inhibition at 0.03 mM
alpha-glycerophosphate
-
-
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
-
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
Benzene
-
at 12.5% (v/v) remaining activity, 88.94%, and 25% (v/v) remaining activity, 88.94%
Chelators
-
-
-
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+
A1YZ23, -
1 mM, 36% decrease of activity
Cu2+
-
complete inhibition of aldolase II above 0.5 mM
Cu2+
A1YZ23, -
1 mM, 57% decrease of activity
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-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
O97447
competitive inhibitor
dihydroxyacetone phosphate
-
-
Dimethylformamid
-
at 12.5% (v/v) remaining activity, 118.40%, and 25% (v/v) remaining activity, 73.93%
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
P67475
1 mM, completely abolishes activity
EDTA
-
0.67 mM, complete inhibition
EDTA
-
0.025 mM and above, no residual activity
EDTA
A1YZ23, -
1 mM, complete inhibition
EDTA
-, Q602L6
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
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%
Fluorescein 5'-isothiocyanate
P53449
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
hydrogen peroxide
-
inhibitory at 0.25%, at pH 7
Hydroquinone diphosphate
-
competitive
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
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-(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-(3-hydroxypropyl)-phosphoglycolohydroxamic acid bis-phosphate
-
-
-
N-hydroxy-2-[(trihydroxyphosphoranyl)oxy]acetamide
-
-
NaBH4
-
in presence of substrate
NaBH4
Chlamydomonas sp.
-
metalloaldolases are indifferent
NaBH4
-
irreversible inactivation
NaBH4
-
inhibition in presence of glycerone phosphate and 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
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
-
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
-
-
Polyphosphate
-
-
pyridoxal 5'-phosphate
-
-
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+
-
complete inhibition of aldolase II above 0.5 mM
[(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
P53449
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 ACCESSION NO.
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
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+
D-glucose
-
about 60% increase of activity
dithiothreitol
-
sulfhydryl compound such as dithiothreitol, activates the C-His-rMtFBA activity slightly, 25%
Nonidet-P40
-
0.5% w/v, enhances activity by 34%
phosphoenolpyruvate
-
enhances D-fructose 1,6-bisphosphate-cleavage activity, fructose 1-phosphate-cleavage activity is unaffected
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00016
-
D-fructose 1,6-bisphosphate
-
-
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
O97447
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
P05062
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
-, Q602L6
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
P05062
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
P05062
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
P05062
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
O97447
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
-, Q602L6
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
P67475
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
P05062
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
P04075
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
P04075
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
P04075
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
-
-
0.1613
-
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
0.3
-
D-fructose 1,6-bisphosphate
-
E181A mutant, 30C
0.3
-
D-fructose 1,6-bisphosphate
-
-
0.305
-
D-fructose 1,6-bisphosphate
Q9RHA2
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
0.43
-
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
A1YZ23, -
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
-, Q602L6
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
-
-
2.7
-
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
P05062
W147R mutant, 22C
0.00173
-
D-Fructose 1-phosphate
P05062
L256P mutant, 22C
0.0022
-
D-Fructose 1-phosphate
P05062
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
P05062
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
P05062
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
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
0.05
-
D-fructose-1,6-bisphosphate
-
-
0.055
-
D-fructose-1,6-bisphosphate
-
-
0.43
-
D-fructose-1,6-bisphosphate
-
at 50C
0.45
-
D-fructose-1,6-bisphosphate
-
-
0.052
-
D-glyceraldehyde 3-phosphate
Q980K6
pH 6.5, 70C
0.19
-
D-glyceraldehyde 3-phosphate
F9VMT6
pH 8.0, 48C, wild-type enzyme
0.34
-
D-glyceraldehyde 3-phosphate
F9VMT6
pH 8.0, 48C, mutant enzyme Y348F
1.17
-
D-glyceraldehyde 3-phosphate
-, Q602L6
in the absence of Co2+, at pH 7.5, 30C
0.0016
-
D-Xylulose 1-phosphate
-
-
0.095
-
dihydroxyacetone phosphate
-, Q602L6
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
P58314, -
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
P58314, -
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
Q980K6
pH 6.5, 70C
0.19
-
glycerone phosphate
F9VMT6
pH 8.0, 48C, wild-type enzyme
0.34
-
glycerone phosphate
F9VMT6
pH 8.0, 48C, mutant enzyme Y348F
0.4
-
glycerone phosphate
-
liver
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
-, Q602L6
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
-
muscle
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0002
-
D-fructose 1,6-bisphosphate
-
turnover number less than 0.0002 sec-1, mutant enzyme K146A
0.001
-
D-fructose 1,6-bisphosphate
-
30C, N286D mutant
0.0019
-
D-fructose 1,6-bisphosphate
-
mutant enzyme K146M
0.002
-
D-fructose 1,6-bisphosphate
-
mutant enzyme D33S
0.0028
-
D-fructose 1,6-bisphosphate
-
30C, D109A mutant
0.003
-
D-fructose 1,6-bisphosphate
-
mutant enzyme D33N
0.005
-
D-fructose 1,6-bisphosphate
-
mutant enzyme E187Q
0.005
-
D-fructose 1,6-bisphosphate
-, Q602L6
in the absence of Co2+, at pH 7.5, 30C
0.011
-
D-fructose 1,6-bisphosphate
-
pH 7.4, 30C, enzyme from patients with intolerance
0.013
-
D-fructose 1,6-bisphosphate
-
E174A mutant, 30C
0.018
-
D-fructose 1,6-bisphosphate
-, 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
F9VMT6
pH 8.0, 48C, mutant enzyme Y348F
0.027
-
D-fructose 1,6-bisphosphate
F9VMT6
pH 8.0, 48C, wild-type enzyme
0.029
-
D-fructose 1,6-bisphosphate
-
pH 7.4, 10C, enzyme from patients with intolerance
0.03
-
D-fructose 1,6-bisphosphate
-
E187Q mutant, pH 7.6, 22C
0.033
-
D-fructose 1,6-bisphosphate
-
E182A mutant, 30C
0.046
-
D-fructose 1,6-bisphosphate
-
mutant enzyme E187A
0.055
-
D-fructose 1,6-bisphosphate
-, 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
-
E187A mutant, pH 7.6, 22C
0.16
-
D-fructose 1,6-bisphosphate
-
N35A mutant, 30C
0.19
-
D-fructose 1,6-bisphosphate
-
pH 7.4, 10C, wild-type enzyme
0.19
-
D-fructose 1,6-bisphosphate
P05062
N334K mutant, 22C
0.19
-
D-fructose 1,6-bisphosphate
-
30C, N286A mutant
0.43
-
D-fructose 1,6-bisphosphate
P05062
W147R mutant, 22C
0.54
-
D-fructose 1,6-bisphosphate
P05062
L256P mutant, 22C
0.57
-
D-fructose 1,6-bisphosphate
P05062
Q354E mutant, 22C
0.58
-
D-fructose 1,6-bisphosphate
-
K325A mutant, 30C
0.61
-
D-fructose 1,6-bisphosphate
P05062
wild-type enzyme, 22C
0.63
-
D-fructose 1,6-bisphosphate
O97447
mutant enzyme D255A, in 50 mM K+-HEPES (pH 7.5), at 25C
0.65
-
D-fructose 1,6-bisphosphate
-
mutant enzyme K107M
0.85
-
D-fructose 1,6-bisphosphate
-
S61A mutant, 30C
1.07
-
D-fructose 1,6-bisphosphate
-
30C, AB_All mutant
1.53
-
D-fructose 1,6-bisphosphate
-
30C, aldolase B
1.53
-
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30C
1.63
-
D-fructose 1,6-bisphosphate
-
pH 5.5
1.69
-
D-fructose 1,6-bisphosphate
-
E189Q mutant, pH 7.6, 22C
2
-
D-fructose 1,6-bisphosphate
-
30C, D144A mutant
2.1
-
D-fructose 1,6-bisphosphate
-
pH 7.4, 30C, wild-type enzyme
2.1
-
D-fructose 1,6-bisphosphate
-
at 30C in 50 mM Tris-HCl, 0.1 M potassium acetate buffer (pH 8.0)
2.2
-
D-fructose 1,6-bisphosphate
-
30C, D288A mutant
2.83
-
D-fructose 1,6-bisphosphate
-
mutant aldolase C Y363S
2.94
-
D-fructose 1,6-bisphosphate
-
E189Q mutant, pH 7.6, 22C
2.94
-
D-fructose 1,6-bisphosphate
-
30C, aldolase B
2.95
-
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30C
3.4
-
D-fructose 1,6-bisphosphate
-
E189A mutant, pH 7.6, 22C
3.55
-
D-fructose 1,6-bisphosphate
-
at pH 7.5 and 25C, in the absence of Zn2+
3.55
-
D-fructose 1,6-bisphosphate
O97447
wild type enzyme, in 50 mM K+-HEPES (pH 7.5), at 25C
4.02
-
D-fructose 1,6-bisphosphate
-
pH 9.3
4.7
-
D-fructose 1,6-bisphosphate
P04075
mutant enzyme G346S
5.03
-
D-fructose 1,6-bisphosphate
-
pH 5.5
5.2
-
D-fructose 1,6-bisphosphate
-
-
5.28
-
D-fructose 1,6-bisphosphate
-
pH 9.2
5.47
-
D-fructose 1,6-bisphosphate
-
pH 7.6
5.8
-
D-fructose 1,6-bisphosphate
-
E181A mutant, 30C
6.08
-
D-fructose 1,6-bisphosphate
-
K325A mutant, 30C
6.08
-
D-fructose 1,6-bisphosphate
P05062
L256P mutant, 22C; Q354E mutant, 22C; wild-type enzyme, 22C
6.08
-
D-fructose 1,6-bisphosphate
-
30C, AB_All mutant
6.3
-
D-fructose 1,6-bisphosphate
-
S61T mutant, 30C
7
-
D-fructose 1,6-bisphosphate
-
30C, D290A mutant
7.5
-
D-fructose 1,6-bisphosphate
-
pH 9.3
7.87
-
D-fructose 1,6-bisphosphate
-
pH 5.5
8.2
-
D-fructose 1,6-bisphosphate
-
30C, wild-type enzyme
8.2
-
D-fructose 1,6-bisphosphate
-
pH 7.6
8.5
-
D-fructose 1,6-bisphosphate
-
Q59A mutant, 30C
10.2
-
D-fructose 1,6-bisphosphate
-
30C, aldolase A
10.2
-
D-fructose 1,6-bisphosphate
-
at 30C
10.3
-
D-fructose 1,6-bisphosphate
-
pH 7.6, native enzyme
10.5
-
D-fructose 1,6-bisphosphate
-
wild-type enzyme, 30C
10.7
-
D-fructose 1,6-bisphosphate
P04075
mutant enzyme E206K
10.9
-
D-fructose 1,6-bisphosphate
-
pH 7.6, recombinant enzyme
12.3
-
D-fructose 1,6-bisphosphate
-
30C, D329A mutant
12.6
-
D-fructose 1,6-bisphosphate
-
aldolase C
13
-
D-fructose 1,6-bisphosphate
-
30C
13.22
-
D-fructose 1,6-bisphosphate
-
native wild type enzyme
13.9
-
D-fructose 1,6-bisphosphate
-
pH 7.6
14
-
D-fructose 1,6-bisphosphate
-
wild-type and mutants, pH 7.4
14.2
-
D-fructose 1,6-bisphosphate
-
30C
15.8
-
D-fructose 1,6-bisphosphate
-
non-muscle-type enzyme
16.5
-
D-fructose 1,6-bisphosphate
-
30C, H156E mutant
16.7
-
D-fructose 1,6-bisphosphate
P04075
wild-type enzyme
16.76
-
D-fructose 1,6-bisphosphate
-
native enzyme, in Tris-HCl buffer (40 mM, pH 8.0), at 25C
17.9
-
D-fructose 1,6-bisphosphate
-
recombinant non-muscle-type enzyme
20.1
-
D-fructose 1,6-bisphosphate
-
aldolase B
20.3
-
D-fructose 1,6-bisphosphate
-
recombinant fusion protein DLF, in Tris-HCl buffer (40 mM, pH 8.0), at 25C
21
-
D-fructose 1,6-bisphosphate
P67475
pH 7.3, 28C
30.1
-
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30C
33
-
D-fructose 1,6-bisphosphate
-
aldolase C
36.9
-
D-fructose 1,6-bisphosphate
-
E189A mutant, pH 7.6, 22C
40
-
D-fructose 1,6-bisphosphate
-
pH 7.5, 30C
42.2
-
D-fructose 1,6-bisphosphate
-
native recombinant enzyme, pH 7.6, 22C
45.7
-
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30C
45.9
-
D-fructose 1,6-bisphosphate
-
-
46
-
D-fructose 1,6-bisphosphate
-
at pH 7.8
46.1
-
D-fructose 1,6-bisphosphate
-
muscle-type enzyme
49.3
-
D-fructose 1,6-bisphosphate
-
recombinant muscle-type enzyme
59.7
-
D-fructose 1,6-bisphosphate
-
aldolase A
64.5
-
D-fructose 1,6-bisphosphate
-
-
0.008
-
D-Fructose 1-phosphate
-
pH 7.4, 30C, enzyme from patients with intolerance
0.019
-
D-Fructose 1-phosphate
-
pH 7.4, 10C, enzyme from patients with intolerance
0.059
-
D-Fructose 1-phosphate
P05062
Q354E mutant, 22C
0.085
-
D-Fructose 1-phosphate
P05062
N334K mutant, 22C
0.12
-
D-Fructose 1-phosphate
-
pH 7.4, 10C, wild-type enzyme
0.25
-
D-Fructose 1-phosphate
P05062
W147R mutant, 22C
0.38
-
D-Fructose 1-phosphate
P05062
L256P mutant, 22C
0.63
-
D-Fructose 1-phosphate
-
30C, aldolase A
0.63
-
D-Fructose 1-phosphate
-
at 30C
0.67
-
D-Fructose 1-phosphate
P05062
wild-type enzyme, 22C
1.47
-
D-Fructose 1-phosphate
-
30C, AB_All mutant
2
-
D-Fructose 1-phosphate
-
pH 7.4, 30C, wild-type enzyme
2.8
-
D-Fructose 1-phosphate
-
-
6.08
-
D-Fructose 1-phosphate
P05062
wild-type enzyme, 22C
6.08
-
D-Fructose 1-phosphate
-
30C, AB_All mutant; 30C, aldolase A; 30C, aldolase B
0.002
-
D-glyceraldehyde 3-phosphate
-, Q602L6
in the absence of Co2+, at pH 7.5, 30C
0.1
-
D-glyceraldehyde 3-phosphate
F9VMT6
pH 8.0, 48C, mutant enzyme Y348F
0.91
-
D-glyceraldehyde 3-phosphate
F9VMT6
pH 8.0, 48C, wild-type enzyme
0.002
-
dihydroxyacetone phosphate
-, Q602L6
in the absence of Co2+, at pH 7.5, 30C
0.167
-
fructose 1-phosphate
-
pH 9.3
0.183
-
fructose 1-phosphate
-
pH 5.5
0.267
-
fructose 1-phosphate
-
pH 7.6
0.45
-
fructose 1-phosphate
-
pH 5.5
0.583
-
fructose 1-phosphate
-
pH 9.3
0.75
-
fructose 1-phosphate
-
mutant aldolase C Y363S
1.05
-
fructose 1-phosphate
-
pH 7.6
1.13
-
fructose 1-phosphate
-
pH 5.5
1.27
-
fructose 1-phosphate
-
pH 9.2
1.28
-
fructose 1-phosphate
-
aldolase A
1.38
-
fructose 1-phosphate
-
muscle-type enzyme
1.48
-
fructose 1-phosphate
-
aldolase C
1.55
-
fructose 1-phosphate
-
recombinant muscle-type enzyme
1.7
-
fructose 1-phosphate
-
pH 7.6
2.67
-
fructose 1-phosphate
-
aldolase C
3.6
-
fructose 1-phosphate
-
non-muscle-type enzyme
3.65
-
fructose 1-phosphate
-
recombinant non-muscle-type enzyme
10.8
-
fructose 1-phosphate
-
aldolase B
0.1
-
glycerone phosphate
F9VMT6
pH 8.0, 48C, mutant enzyme Y348F
0.003
-
sedoheptulose 1,7-bisphosphate
-, Q602L6
in the absence of Co2+, at pH 7.5, 30C
25.2
-
sedoheptulose 1,7-diphosphate
-
-
33.3
-
sedoheptulose 7-phosphate
-
pH 7.5, 30C
0.91
-
glycerone phosphate
F9VMT6
pH 8.0, 48C, wild-type enzyme
additional information
-
additional information
-
-
-
additional information
-
additional information
-
turnover-numbers of wild-type and mutant enzymes
-
additional information
-
additional information
-
Km for fructose 1,6-diphosphate is dependent on the protein concentration in the range 0.01-0.05 mM
-
additional information
-
additional information
-
turnover-numbers of chimeric enzymes between two human aldolases A, B, or C
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.066
-
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30C
9138
0.44
-
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30C
9138
9
-
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30C
9138
10.8
-
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30C
9138
40
-
D-fructose 1,6-bisphosphate
O97447
mutant enzyme D255A, in 50 mM K+-HEPES (pH 7.5), at 25C
9138
1080
-
D-fructose 1,6-bisphosphate
-
recombinant fusion protein DLF, in Tris-HCl buffer (40 mM, pH 8.0), at 25C
9138
1160
-
D-fructose 1,6-bisphosphate
-
native enzyme, in Tris-HCl buffer (40 mM, pH 8.0), at 25C
9138
2000
-
D-fructose 1,6-bisphosphate
O97447
wild type enzyme, in 50 mM K+-HEPES (pH 7.5), at 25C
9138
0.29
-
D-glyceraldehyde 3-phosphate
F9VMT6
pH 8.0, 48C, mutant enzyme Y348F
9226
4.7
-
D-glyceraldehyde 3-phosphate
F9VMT6
pH 8.0, 48C, wild-type enzyme
9226
0.29
-
glycerone phosphate
F9VMT6
pH 8.0, 48C, mutant enzyme Y348F
11085
4.7
-
glycerone phosphate
F9VMT6
pH 8.0, 48C, wild-type enzyme
11085
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
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
1.3e-05
-
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
-
-
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
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
1e-05
-
phosphoglycolo hydroxamic acid
-
-
1e-05
-
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]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.33
-
5-chloro-8-hydroxyquinoline
-
NADH-linked enzymatic assay
0.533
-
5-chloro-8-hydroxyquinoline
-
determined by the colorimetric assay
0.02
-
5-formyl-6-hydroxynaphthalen-2-yl dihydrogen phosphate
-
15 min incubation time
0.496
-
8-hydroxyquinoline
-
NADH-linked enzymatic assay
0.5
-
8-hydroxyquinoline
-
determined by the colorimetric assay
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.01
-
-
substrate: D-fructose 1,6-bisphosphate, 50C, pH not specified in the publication, enzyme from starch-grown cells
0.123
-
-
after 1fold purification, at 25C
0.13
-
P05062
N334K mutant, D-fructose 1-phosphate as substrate
0.28
-
P05062
N334K mutant, D-fructose 1,6-bisphosphate as substrate
0.3
-
-
-
0.38
-
P05062
W147R mutant, D-fructose 1-phosphate as substrate
0.58
-
P05062
L256P mutant, D-fructose 1-phosphate as substrate
0.64
-
P05062
W147R mutant, D-fructose 1,6-bisphosphate as substrate
0.81
-
P05062
L256P mutant, D-fructose 1,6-bisphosphate as substrate
0.86
-
P05062
Q354E mutant, D-fructose 1,6-bisphosphate as substrate
0.88
-
P05062
Q354E mutant, D-fructose 1-phosphate as substrate
0.94
-
P05062
wild-type enzyme, D-fructose 1-phosphate as substrate
0.97
-
P05062
wild-type enzyme, D-fructose 1,6-bisphosphate as substrate
3.2
-
-
enzyme form I
4.8
-
-
enzyme form II
5.3
-
-
strain 168, spore
5.92
-
-
muscle-type enzyme
6.1
-
P04075
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
-
-
-
15.1
-
-
-
15.7
-
P04075
mutant enzyme E206K
16.1
-
-
-
17.27
-
-
liver enzyme
18.5
-
-
recombinat muscle-type enzyme
20
-
-
class I aldolase
22
-
-
class II aldolase
22.3
-
P04075
wild-type enzyme
25.5
-
-
-
26.7
-
-
splitting of fructose 1,6-bisphosphate
29.86
-
-
-
32.3
-
-
strain PCI 219, spore
34.85
-
-
purified native-rMtFBA
35.05
-
-
purified C-His-rMtFBA
44.29
-
-
-
46
-
Q9RHA2
-
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
9
-
-
6
8.5
-
class I aldolase
6
-
-
at 22C
6
-
-
E187A and E189Q mutant
6.5
8.5
-
with D-fructose 1,6-bisphosphate as substrate
6.5
9
-
aldolase I
6.5
-
Q980K6
assay at
6.8
-
-
at 5C
7
7.5
-
class II aldolase
7
-
-
cleavage of fructose 1-phosphate
7
-
-
-
7
-
P53449
assay at
7.3
-
-
soluble enzyme
7.4
7.8
-
-
7.4
-
-
cleavage of D-fructose 1,6-bisphosphate
7.5
-
-
with fructose 1-phosphate as substrate
7.5
-
-
immobilized enzyme
7.5
-
-
-
7.5
-
-
-
7.5
-
-
-
8
-
-
-
8
-
-
broad, plastidic and cytosolic enzyme
8
-
-
broad optimum, wild-type and E189A mutant
8.5
9.5
-
-
8.5
-
A1YZ23, -
-
8.6
-
-
aldolase class II
9
9.5
-, Q602L6
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
P67475
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
P53449
assay at
40
-
-
soluble enzyme
45
-
-
immobilized enzyme
50
-
P58314, -
assay at
50
-
-
assay at
50
-
-
assay at, temperature optimum for the specific acitivity of MJ0400-His6
50
-
-
assay at
60
-
A1YZ23, -
-
70
-
Q980K6
assay at
80
-
Q9RHA2
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
-
Q9RHA2
little activity below
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-, Q9U9R9
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
-, Q9U9R9
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
B5B3T4, -
weak expression
Manually annotated by BRENDA team
-
tail muscle
Manually annotated by BRENDA team
P53449
breast
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
B5B3T4, -
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
B5B3T4, -
weak expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
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
PDB
SCOP
CATH
ORGANISM
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Coccidioides immitis (strain RS)
Encephalitozoon cuniculi (strain GB-M1)
Encephalitozoon cuniculi (strain GB-M1)
Encephalitozoon cuniculi (strain GB-M1)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Helicobacter pylori (strain 51)
Helicobacter pylori (strain 51)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Thermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1)
Thermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1)
Thermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1)
Thermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1)
Thermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30900
-
A1YZ23, -
calculated from sequence of cDNA
33000
-
-
gel filtration
33090
-
Q9RHA2
monomeric form, calculated from amino acid sequence
34000
-
-
sucrose density gradient centrifugation
35380
-
-
calculated from amino acid sequence
37000
-
-
purified native-rMtFBA
38000
-
-
purified C-His-rMtFBA
38000
-
-
SDS-PAGE
39000
-
-
SDS-PAGE
39600
-
Q1HDV3
SDS-PAGE
39600
-
Q1HDV2
SDS-PAGE
40000
60000
-
gel filtration, monomeric form, A149P, N334K, L256P, A337V mutant
40000
-
-
SDS-PAGE
40000
-
-
silver-stained SDS-PAGE two bands of about 40 and 80 kDa, 40 kDa monomeric form
41000
-
-, Q9U9R9
SDS-PAGE
44000
-
-
SDS-PAGE
44000
-
-
SDS-PAGE
44000
-
P53442, -
SDS-PAGE
45000
-
-
SDS-PAGE
45000
-
-
gel filtration
53000
-
-
gel filtration
57000
-
-
sucrose density gradient centrifugation, 30C
70000
-
-
SDS-PAGE
70000
-
-
gel filtration
71000
-
-
sucrose density gradient centrifugation, 4C
77760
-
-
analytical ultracentrifugation
78000
-
-
ultracentrifugal analysis
79290
-
-
ESI mass spectrometry
79300
-
-
gel filtration
80000
-
-
gel filtration
80000
-
-
aldolase II, gel filtration
80000
-
-
silver-stained SDS-PAGE two bands of about 40 and 80 kDa, 80 kDa dimeric form
120000
-
-
determination of sedimentation velocity
120000
-
-
sucrose density gradient centrifugation
120000
-
-
liver enzyme, gel filtration
137000
-
-
sucrose density gradient centrifugation
138000
-
Q9RHA2
nondenaturating PAGE
140000
-
-
gel filtration
140000
-
-
gel filtration
142000
160000
-
ultracentrifugation experiments
142000
-
-
gel filtration
143000
-
-
cytosolic enzyme, sucrose density gradient centrifugation
148000
-
-
chloroplastic enzyme, method of Martin and Ames
150000
-
-
gel filtration
150000
-
-
-
158000
-
-
sedimentation equilibrium ultracentrifugation
158000
-
-
gel filtration
158000
-
-
sedimentation equilibrium ultracentrifugation
158000
-
-
gel filtration, W147R, R303W, A337V mutant
158000
-
Q9RHA2
gel filtration
158000
-
P67475
gel filtration
159000
-
-
gel filtration
159000
-
-
gel filtration
159000
-
-
gel filtration
160000
175000
-
gel filtration, multiangle laser light scattering
160000
-
-
gel filtration, equilibrium sedimentation
160000
-
-
gel filtration
160000
-
-
glycerol density gradient centrifugation
160000
-
-
class I aldolase, gel filtration
160000
-
-
gel filtration
162000
-
-
gel filtration
165000
-
-
gel filtration
165000
-
-
gel filtration
165000
-
-
-
170000
-
-
recombinant aldolase B, gel filtration
170000
-
P05062
tetrameric form, gel filtration
170000
-
P04075
gel filtration
240000
-
-, Q602L6
gel filtration
241000
-
-
gel filtration
272000
-
P58314, -
gel filtration
340000
-
-
ultracentrifugal analysis
additional information
-
-
structure and amino acid composition
additional information
-
-
L256P mutant exists as tetramer partly dissociated into its subunits, A149P and N334K exist as mixture of protein conformers that encompass all molecular sizes between tetramer and monomer
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 36700, SDS-PAGE
?
-
x * 38000, chloroplastic isoenzyme, SDS-PAGE; x * 40000, cytosolic isoenzyme, SDS-PAGE
?
-
x * 35000, enzyme form I, SDS-PAGE; x * 37000, enzyme form II, SDS-PAGE
?
-
x * 40000, cytosolic isoenzyme, SDS-PAGE
?
-
x * 40000, SDS-PAGE
dimer
-
2 * 38500, SDS-PAGE
dimer
-
gel filtration, enzyme from patients with fructose intolerance
dimer
-
A149P and N334K mutants exist as mixture of protein conformers that encompass all molecular sizes between tetramer and monomer
dimer
-
2 * 39026, electrospray ionization mass spectrometry
dimer
-
rabbit muscle D128V aldolase. The D128V mutation causes aldolase to lose intermolecular contacts with the neighbouring subunit at one of the two interfaces of the tetramer
dimer
-
to identify proteins that interact with the MADS domain protein NMH7 of Medicago sativa, an affinity column is used with a synthetic peptide derived from the MADS domain of NMH7 which mediate protein-protein interaction with non-MADS domain interacting proteins. Identification of proteins as the monomeric and dimeric forms of fructose-1,6-bisphosphate aldolase cytosolic class I
heterodimer
-
1 * 30671 + 1 * 30540, mass spectrometry
heterodimer
-
1 * 39775 + 1 * 39644, mass spectrometry
heterodimer
-
1 * 30671 + 1 * 30540, mass spectrometry
-
homodimer
-
2 * 35000, gel filtration
homodimer
-
x-ray crystallography
homodimer
-
2 * 39650, gel filtration
homohexamer
-, Q602L6
6 * 38500, calculated from amino acid sequence; 6 * 40000, SDS-PAGE
homotetramer
-
4 * 36411, mass spectrometry
homotetramer
-
4 * 38441, mass spectrometry
monomer
-
1 * 33000
monomer
-
1 * 33000, SDS-PAGE
monomer
-
1 * 33000, SDS-PAGE
monomer
-
A149P and N334K mutants exist as mixture of protein conformers that encompass all molecular sizes between tetramer and monomer
monomer
-
to identify proteins that interact with the MADS domain protein NMH7 of Medicago sativa, an affinity column is used with a synthetic peptide derived from the MADS domain of NMH7 which mediate protein-protein interaction with non-MADS domain interacting proteins. Identification of proteins as the monomeric and dimeric forms of fructose-1,6-bisphosphate aldolase cytosolic class I
octamer
P58314, -
8 * 31100, SDS-PAGE
octamer
-
8 * 28700, SDS-PAGE
tetramer
-
4 * 30000
tetramer
-
4 * 40750, SDS-PAGE
tetramer
-
4 * 30000, SDS-PAGE
tetramer
-
4 * 41000, SDS-PAGE
tetramer
-
4 * 30000, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE, equilibrium sedimentation in 6 M guanidine/HCl, SDS-PAGE
tetramer
-
4 * 35000, chloroplastic enzyme, SDS-PAGE; 4 * 38000, cytosolic enzyme, SDS-PAGE
tetramer
-
-
tetramer
-
4 * 42000, SDS-PAGE
tetramer
-
4 * 37800, SDS-PAGE
tetramer
-
4 * 38000, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
tetramer
-
4 * 38000, recombinant aldolase A and liver enzyme, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
tetramer
-
4 * 40000, class I aldolase, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
tetramer
-
4 * 34000, SDS-PAGE
tetramer
-
crystallographic data
tetramer
-
4 * 40000, SDS-PAGE
tetramer
P05062
-
tetramer
-
L256P mutant exists as tetramer partly dissociated into its subunits, A149P and N334K exist as mixture of protein conformers that encompass all molecular sizes between tetramer and monomer
tetramer
Q9RHA2
4 * 33000, SDS-PAGE
tetramer
Q703I2, -
x-ray crystallography
tetramer
-
x-ray crystallography
tetramer
-
wild-type
trimer
-
A149P and N334K mutants exist as mixture of protein conformers that encompass all molecular sizes between tetramer and monomer
monomer
Peptoniphilus asaccharolyticus 228
-
1 * 33000
-
additional information
P05062
A149P mutant shows tetrameric and monomeric forms and other species with molecular masses intermediate between those corresponding to the tetramer and monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
class II aldolase in complex with phosphoglycolohydroxamate
-
with Cd2+ in place of Zn2+
-
D83A and D255A mutant enzymes, hanging drop vapor diffusion method, using 18-25% (w/v) glycol 3350 and 0.2 M NH4NO3
O97447
hanging drop vapour diffusion method with 18-23% polyethylene glycol monomethyl ether 2000, 0.1 M Tris-HCl (pH 8.8), and 0.2 M MgCl2
-
in complex with ([3-hydroxy-2-oxo-4-[2-(phosphonooxy)ethyl]pyridin-1(2H)-yl]methyl)phosphonic acid, hanging drop vapor diffusion method, using 22% (w/v) polyethylene glycol 3350 and 0.2 M NH4NO3
-
complex of aldolase and dihydroxyacetone phosphate Schiff-base, hanging drop vapor diffusion method
-
hanging drop vapor diffusion method, structure is solved at 3.0 A resolution
-
vapour diffusion method using 15% polyethylene glycol 5000 MME in 20 mM sodium phosphate pH 4.0
-
complexed with fructose 1,6-bisphosphate
-
D33N and D33S mutant enzymes
-
hanging-drop vapor-diffusion method
-
in complex with dihydroxyacetone phosphate
-
recombinant enzyme, vapour diffusion method. Crystal structures are determined to 1.8 resolution of fructose-1,6-bis(phosphate) aldolase trapped in complex with its substrate and a competitive inhibitor, mannitol-1,6-bis(phosphate). The enzyme substrate complex corresponds to the postulated Schiff base intermediate and has reaction geometry consistent with incipient C3-C4 bond cleavage catalyzed by Glu187, which is adjacent to the Schiff base-forming Lys229
-
vapor diffusion method and/or batch crystallization
-
sitting-drop vapour-diffusion method at 25C, crystallization of the enzyme in the presence of glycerone phosphate and Mg2+, determination of the crystal structure at 1.5 A resolution. Crystal structure of the bifunctional enzyme (fructose-bisphosphate aldolase/fructose-bisphosphatase) at 1.5 A resolution in the aldolase form, where a critical lysine residue forms a Schiff base with glycerone phosphate. A structural comparison of the aldolase form with a phosphatase form reveals a dramatic conformational change in the active site, demonstrating that the enzyme metamorphoses its active-site architecture to exhibit dual activities
F9VMT6
crystal structures of Y146F covalently bound to the carbinolamine intermediate of the substrate fructose 1,6-bisphosphate and noncovalently bound to the cyclic form of the substrate. The structures are determined at a resolution of 1.9 A and refined to crystallographic R factors of 0.148 and 0.149, respectively. The crystal structure of the W144E/Y146F double-mutant substrate complex represents the first example where the cyclic form of beta-fructose 1,6-bisphosphate is noncovalently bound to FBPA I
-
the crystal structure of the archaeal FBPA revealed that the protein fold is that of a parallel (betaalpha)8 barrel
-
hanging and sitting drop vapor diffusion method
-
hanging drop vapour diffusion method using 27% polyethylene glycol 10000, 0.1M HEPES-NaOH, at pH 7.0-7.5
Q703I2, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1
12
-
5 min, stable
4
5
-
80% loss of activity, irreversible
5
-
-
30 min, 90% loss of activity
5.4
9.4
-
25C, 22 h, enzyme concentration: 0.27 mg/ml, less than 30% loss of activity, recombinant enzyme
6
7.5
-
maximal thermal stability in the pH-range, soluble enzyme
7
10
-
C-His-rMtFBA and native-rMtFBA are stable in a wider pH range of 7.0-10.0
7
7.5
-
maximal thermal stability in the pH-range, immobilized enzyme
10
-
-
30C, 15 min, 5% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
-
-
enzyme from patients with fructose intolerance shows increased temperature sensitivity, activity at 10C is 6fold lower than that of the wild-type, and activity decreases substantially at higher temperatures
25
-
-
3 d, 25% loss of activity
30
55
-
activity lost substantially at higher temperature
30
80
-, Q602L6
the enzyme activity is retained after incubation for 2 h at 30, 40, or 50C, respectively. The half-life of the enzyme is 1 h at 60C, and the enzyme is fully inactivated after heating at 80C for 10 min
30
-
-
pH 10, 15 min, 5% loss of activity
37
-
-
native enzyme is completely stable
37
-
-
pH 7.4, 30 min, stable
40
-
P05062
W147R melting temperature of W147R mutant and L256P mutant is 40C versus 47C for the wild-type enzyme
45
60
-
the aldolase loses 25% of its activity after 10 min of incubation at 45C and loses almost all its activity after a10 min incubation at 60C
45
-
-
stable for 60 min
47
-
P05062
melting temperature of the wild-type enzyme
48
-
P04075
melting temperature of mutant E206K
50
-
-
pH 7.0, 10 min, stable up to
50
-
-
chloroplastic enzyme, half-life: 3 min
50
-
-
about 10% loss of activity of soluble enzyme and immobilized enzyme after 100 min
50
-
-
30 min, about 40% loss of aldolase C activity with D-fructose 1,6-bisphosphate as substrate; 30 min, about 5% loss of aldolase A activity with D-fructose 1,6-bisphosphate as substrate; 30 min, about 70% loss of aldolase B activity with D-fructose 1,6-bisphosphate as substrate; 30 min, about 80% loss of aldolase C activity with fructose 1-phosphate as substrate
50
-
-
5 min, stable
50
-
-
23 min, 50% loss of activity
50
-
-
8 min, 50% loss of activity
50
-
-
14 min, 50% loss of activity
50
-
-
8 min, 5% loss of activity
50
-
-
30 min, complete loss of activity
50
-
-
50% loss of activity after incubation for 10 min at 49.5C
51
-
-
50% loss of activity after incubation for 10 min at 50.5C
54
-
P04075
melting temperature of wild-type enzyme is 54.4C
55
-
-
about 10% loss of activity of the immobilized enzyme after 100 min; about 25% loss of activity of the soluble enzyme after 100 min
55
-
-
3 min, 33% loss of activity
55
-
P04075
melting temperature of mutant enzyme G346S is 54.8C
60
-
-
pH 7.0, 10 min, about 15% loss of activity with D-fructose 1,6-bisphosphate
60
-
-
about 25% loss of activity of the immobilized enzyme after 100 min; about 50% loss of activity of the soluble enzyme after 100 min
60
-
-
30 min, about 90% loss of aldolase A activity with D-fructose 1,6-bisphosphate as substrate
60
-
-
5 min, 22% loss of activity
60
-
-
pH 7.5, less than 30% loss of activity
60
-
-
3 min, 50% loss of activity
60
-
-
5 min, complete loss of activity
60
-
-
the aldolase loses almost all its activity after a 10 min incubation at 60C
60
-
-
the aldolase loses almost all its activity after a10 min incubation at 60C
65
-
-
10 min, complete inactivation
65
-
-
complete inactivation of the soluble enzyme after 40 min, complete inactivation of the immobilized enzyme after 70 min
80
-
-
pH 7.0, 10 min, about 35% loss of activity with D-fructose 1,6-bisphosphate
80
-
-
2 h, stable
80
-
Q9RHA2
stable for 45 min
80
-
-
very sensitive to moist heat at 80C
90
93
-
half-life: 2 h
90
-
-
pH 7.0, 10 min, complete loss of activity with D-fructose 1,6-bisphosphate
90
-
-
2 h, stable
90
-
-
FBPA shows an almost complete recuperation (92%) of the secondary structure after denaturation at 90C
90
-
-
the aldolase retains almost half of its activity after 10 min of incubation at 90C
95
-
-
half-life: 46 min
97
-
-
90 min, stable
97
-
-
1 h, 80% loss of activity. Half-life: 16 min
100
-
-
complete inactivation after more than 90 min
100
-
-
the enzyme survives boiling for 1 h
120
-
-
20 min, about 20% loss of activity
130
-
-
10 min, complete inactivation
additional information
-
-
phosphate and 2-mercaptoethanol protect against thermal inactivation
additional information
-
-
-
additional information
-
-
10% w/v ethanol results in 2fold reduction in thermal stability
additional information
-
-
displays heat stability with a half-life of 1 h at 100C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
high degree of stability towards frequent freezing and thawing
-
carboxypeptidase A treatment results in 20% inactivation. Complete protection by D-fructose 1,6-bisphosphate
-
stored in the 50 mM Tris-HCl buffer, pH 7.4 containing 1 mM 2-mercaptoethanol and 100 microM ZnCl2, stable at 4C for over 10 months without significant loss of activity.
-
at 1-4 M urea, slight decrease in activity of the immobilized enzyme. In 5 M urea significant decrease in activity after 2 h. In 3 M urea the soluble enzyme unfolded and dissociated totally during 2 h
-
immobilization by covalent attachment to a polyacrylamide matrix containing carboxylic functional groups increases stability
-
10% w/v ethanol results in 2fold reduction in thermal stability
-
freezing inactivates
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acetone
-
more than 50% of the enzyme activity is retained in the presence of 25% (v/v) acetone
Acetone
-
more than 50% of the enzyme activity is retained in the presence of 10% (v/v) acetone
Acetone
-
more than 50% of the enzyme activity is retained in the presence of 25% (v/v) acetone
Acetone
-
more than 50% of the enzyme activity is retained in the presence of 25% (v/v) acetone
-
acetonitrile
-
more than 50% of the enzyme activity is retained in the presence of 10% (v/v) acetonitrile
acetonitrile
-
more than 50% of the enzyme activity is retained in the presence of about 5% (v/v) acetonitrile
acetonitrile
-
more than 50% of the enzyme activity is retained in the presence of 10% (v/v) acetonitrile
acetonitrile
-
more than 50% of the enzyme activity is retained in the presence of 15% (v/v) acetonitrile
acetonitrile
-
more than 50% of the enzyme activity is retained in the presence of 10% (v/v) acetonitrile
-
dimethylformamide
-
more than 50% of the enzyme activity is retained in the presence of 50% (v/v) dimethylformamide
dimethylformamide
-
more than 50% of the enzyme activity is retained in the presence of 10% (v/v) dimethylformamide
dimethylformamide
-
more than 50% of the enzyme activity is retained in the presence of 20% (v/v) dimethylformamide
dimethylformamide
-
more than 50% of the enzyme activity is retained in the presence of 35% (v/v) dimethylformamide
dimethylformamide
-
more than 50% of the enzyme activity is retained in the presence of 50% (v/v) dimethylformamide
-
DMSO
-
167% activity in the presence of 50% (v/v) DMSO
DMSO
-
more than 50% of the enzyme activity is retained in the presence of 20% (v/v) DMSO
DMSO
-
more than 50% of the enzyme activity is retained in the presence of 50% (v/v) DMSO
DMSO
-
167% activity in the presence of 50% (v/v) DMSO
-
tert-Butanol
-
more than 50% of the enzyme activity is retained in the presence of about 5% (v/v) tert-butanol
tert-Butanol
-
more than 50% of the enzyme activity is retained in the presence of 20% (v/v) tert-butanol
tert-Butanol
-
more than 50% of the enzyme activity is retained in the presence of 15% (v/v) tert-butanol
tert-Butanol
-
more than 50% of the enzyme activity is retained in the presence of about 5% (v/v) tert-butanol
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, in 50 mM HEPES buffer with pH 7.3 supplemented with ZnCl2, 24 h, 40% loss of activity
-
-10C, stable for up to 12 months
-
-20C, 50% v/v glycerol/20 mM TrisHCl, stable for at least 1 month
P04075
-20C, wild-type and Q354E mutant: stable in 50% glycerol for 1 month, W147R and L256P mutant enzyme: aggregate after 15 days suggesting structural instability
P05062
4C, 20 mM Tris/HCl, pH 7.4, stable for at least 2 weeks
P04075
wild-type enzyme: 50% loss of activity after 3 months, mutants: accelerated loss of activity
-
-20C, stable for 3 weeks
-
-20C, stable for 4 weeks
-
4C, in 50 mM HEPES buffer with pH 7.3 supplemented with ZnCl2, several days, the enzyme remains stable
-
4C, 5% loss of activity after 1 year
-
0C, pH 8.0, 72% loss of activity after 5 days
-
4C, no loss of activity after 2 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
nickel affinity chromatography
A1YZ23, -
ammonium sulfate precipitation, DEAE Sepharose column chromatography, and Sepharose Q column chromatography
-
5 isoenzymes: A4, A3C1, A2C2, A1C3 and C4
-
Ni2+ affinity chromatography
-
enzyme form I and II
-
Ni-nitrilotriacetic acid agarose column chromatography
-
DEAE-52 column chromatography and Superose-12 column chroatography
-
class II enzyme
-
class I aldolase and class II aldolase
-
Sepharose Q chromatography, Sephacryl 100 gel filtration, and phenyl-Sepharose chromatography
-
ammonium sulfate precipitation, DEAE-Toyopearl 650 S column chromatography, and TSKgel Phenyl 5PW column chromatography
-
95% homogeneity
P05062
95% pure
-
enzyme from patients with fructose intolerance
-
homogeneity
-
normal and chimeric enzymes
-
partial
-
recombinant aldolase B and liver enzyme
-
recombinant wild-type and mutant enzymes G346S and E206K
P04075
MonoQ-Sepharose column chromatography and gel filtration
-
phenyl-Sepharose column chromatography
-
nickel chelating affinity chromatography and gel filtration
-
ammonium sulfate fractionation, DEAE Sepharose CL-6B resin chromatography, and Resource Q column chromatography
-
ammonium sulfate precipitation, DEAE Sepharose column chromatography, and Sepharose Q column chromatography
-
Ni2+-NTA column chromatography
-, Q602L6
ammonium sulfate precipitation, DEAE Sepharose column chromatography, and Sepharose Q column chromatography
-
immobilized metal affinity chromatography, Ni2+-IDA affinity chromatography
-
recombinant
P67475
HisPur cobalt resin column chromatography
-
CM-Sepharose CL-6B chromatography
-
phenyl-Sepharose column chromatography and hydroxylapatite chromatography
-
ammonium sulfate precipitation, DEAE Sepharose column chromatography, and Sepharose Q column chromatography
-
recombinant protein
P58314, -
purification of the recombinant FBPA
Q1HDV2
glutathione Sepharose 4B, electro elution procedure
P53442, -
recombinant enzyme
-
HisTrap column chromatography
B5B3T4, -
nickel/iminodiacetic acid agarose column chromatography and Superdex 75 gel filtration
-
class I and class II aldolase
-
recombinant protein
-
near homogeneity
Q9RHA2
recombinant enzyme
-
simultaneous purification of EC 2.7.1.1, EC 4.1.2.13, EC 5.3.1.1, and EC 2.7.2.3
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS cells
A1YZ23, -
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli
-
expressed in Escherichia coli
-
3 isoenzymes: alpha, beta and gamma. Expression in Escherichia coli
-
cytosolic and plastidic enzyme
-
expressed in Escherichia coli strain BL21(DE3)Star
-
expressed in Escherichia coli
-
aldolase C, expression in Escherichia coli
-
enzyme from patients with fructose intolerance
-
expressed in Escherichia coli
-
wild-type enzyme and mutant enzymes G346S and E206K, expression in Escherichia coli
P04075
expressed in Escherichia coli
-
expressed in Escherichia coli BL21pLysS cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli strain strain Bl21(DE3), vector pT7-7
-
expressed in Escherichia coli
-
cloning, overexpression of C-terminally His-tagged MJ0400 enzyme in Escherichia coli Rosetta2(DE3)pLysS cells
-
expressed in Escherichia coli BL21(DE3) cells
-, Q602L6
expressed C-terminal histidine-tagged Class II FBA is produced in Escherichia coli BL21
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
subcloned in the Escherichia coli vector pT7-7. Attempts to express the enzyme with an N-terminal fusion tag yields inactive, mostly insoluble protein
P67475
TOP10F' and BL21(DE3) pLysS are used for the expression of 6x histidine-tagged recombinant enzyme encoded by plasmid pSAT-FBA
-
fusion protein with glutathione S-transferase
-, Q9U9R9
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 SI cells
-
expressed in Anabaena sp. strain PCC 7120
-
expression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli
P58314, -
expressed in Escherichia coli BL21 cells
-
cloned into a pQE-30 vector and inserted into Escherichia coli JM-109 for expression
Q1HDV3
expression of the recombinant FBPA in Escherichia coli JM-109
Q1HDV2
expressed in Escherichia coli as a fusion protein (GST/P44)
P53442, -
expressed in Escherichia coli strain BL121
B5B3T4, -
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression in Escherichia coli
Q980K6
overexpression of Sll1330 in Escherichia coli
Q55664
expressed in Escherichia coli
-
expressed in Escherichia coli
-
overexpression in Escherichia coli
-
expressed in Escherichia coli
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
on stimulation with epidermal growth factor, the wound recovery area and ALDOA and its mRNA levels increase
-
abiotic stimuli such as seawater, 500 mM/l NaCl, 0.1 M abscisic acid, and PEG 8000 (20% w/v) can trigger a significant induction of FBA in Sesuvium portulacastrum roots within 2-12 h
B5B3T4, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K232R
-
the mutant protein has lost FBP aldolase activity, whereas the FBP phosphatase activity is 3fold enhanced
D109A
-
very low catalytic activity
D144A
-
increased Km
D288A
-
increased Km
D290A
-
increased Km
D329A
-
increased Km
E174A
-
severely crippled catalysis
E181A
-
mutant enzyme has wild-type properties
E182A
-
decrease in kcat
N286A
-
increased Km, decreased kcat
N286D
-
increased Km, severely decreased kcat
N35A
-
1.56% activity of the wild-type enzyme
Q59A
-
no significant effect on enzyme function
S61A
-
increased Km for fructose 1,6-bisphosphate
S61T
-
no effect on catalysis
D255A
O97447
the mutation results in an enzyme that possesses double specificity, now cleaving D-tagatose 1,6-bisphosphate (albeit with low efficacy) while maintaining activity toward D-fructose 1,6-bisphosphate at a 50fold lower catalytic efficacy compared with that of wild type FBPA
D83A
-
impaired enzyme activity
D83A
O97447
inactive
A149P
P05062
no catalytic activity
A149P
-
tetramers dissociate into subunits with greatly impaired enzymatic activity
A174D
-
tetramers dissociate into subunits with greatly impaired enzymatic activity, extremely labile mutant, aggregates rapidly
A337V
-
retained tetrameric structure, altered kinetic properties
C239A
-
activity similar to wild-type enzyme, more stable in long-term storage at 25C
C289A
-
activity similar to wild-type enzyme, more stable in long-term storage at 25C
C338A
-
activity similar to wild-type enzyme, more stable in long-term storage at 25C
C72A
-
activity similar to wild-type enzyme, more stable in long-term storage at 25C
E206K
P04075
mutant has a KM-value 2fold higher than that of both the Gly346S mutant and the wild-type enzyme, and a turnover-number value 40% less than the wild-type
G346S
P04075
mutant enzyme has the same KM-value as the wild-type enzyme, but a 4fold lower turnover-number
L256P
P05062
melting temperature is 40C versus 47C for the wild-type enzyme
N334K
P05062
increased Km value
N334K
-
tetramers dissociate into subunits with greatly impaired enzymatic activity
Q354E
P05062
kinetis resemble that of the wild-type enzyme
R303W
-
retained tetrameric structure, altered kinetic properties
W147R
P05062
melting temperature is 40C versus 47C for the wild-type enzyme
W147R
-
retained tetrameric structure, altered kinetic properties
Y363S
-
Y363S has reduced catalytic activity towards D-fructose 1,6-bisphosphate and fructose 1-phosphate
G312A
-
mutation does not perturb ligand binding in the active site
C-His-rMtFBA
-
C-terminal histidine-tagged Class II FBA
D128V
-
mutation, mimicking the clinically important D128G mutation in humans
D33N
-
the mutation drastically reduces the rate of turnover but does not impact substrate binding
D33S
-
the mutation drastically reduces the rate of turnover but does not impact substrate binding
E187A
-
mutation compromises enzyme activity
E187A
-
the mutation drastically reduces the rate of turnover
E187Q
-
K107M, K146M, K229M, K229A and E187Q, have decreased cleavage activity towards D-fructose 1,6-bisphosphate
E187Q
-
mutation compromises enzyme activity
E187Q
-
the mutation drastically reduces the rate of turnover
E189A
-
almost no loss in catalytic activity
E189Q
-
only small loss in catalytic activity
H156E
-
similar kinetics and stability as wild-type enzyme
K107M
-
K107M, K146M, K229M, K229A and E187Q, have decreased cleavage activity towards D-fructose 1,6-bisphosphate
K107M
-
46fold increase in Ki-value for naphthyl 2,6-bisphosphate, 11.5fold increase in KM-value for D-fructose 1,6-diphosphate. The structure of the enzyme is isomorphous with respect to wild-type enzyme
K107M
-
the mutation drastically reduces the rate of turnover
K146A
-
is unable to cleave the C3-C4 bond of the hexose while retaining the ability to form the covalent intermediate, although at a greatly diminished rate
K146A
-
the mutation drastically reduces the rate of turnover
K146M
-
K107M, K146M, K229M, K229A and E187Q, have decreased cleavage activity towards D-fructose 1,6-bisphosphate
K146M
-
decrease in rate of complex formation between enzyme and inhibitor 1-hydroxy-2-naphthaldehyde 6-phosphate, but no change in ability to form the complex
K146M
-
mutant with severely compromised catalytic activity
K146M
-
the mutation drastically reduces the rate of turnover
K229A
-
K107M, K146M, K229M, K229A and E187Q, have decreased cleavage activity towards D-fructose 1,6-bisphosphate
K229M
-
K107M, K146M, K229M, K229A and E187Q, have decreased cleavage activity towards D-fructose 1,6-bisphosphate
S271
-
mutation decreases by 1 order of magnitude the affinity of 1-hydroxy-2-naphthaldehyde 6-phosphate for the aldolase active site but does not modify its ability to catalyze Schiff base formation
Y229F
F9VMT6
the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 1.1fold higher than the wild-type value, no fructose-bisphosphate aldolase activity
Y348F
F9VMT6
the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 3.5fold lower than the wild-type value, the kcat/Km-value for the fructose-bisphosphate aldolase reaction of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) in the anabolic direction is 16fold lower than wild-type value
Y229F
Sulfolobus tokodaii 7
-
the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 1.1fold higher than the wild-type value, no fructose-bisphosphate aldolase activity
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Y146F
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catalytically deficient mutant
K156M
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identical to wild type enzyme
K16M
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not inhibited by 5-formyl-6-hydroxynaphthalen-2-yl dihydrogen phosphate
K239M
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identical to wild type enzyme
additional information
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methionine/cysteine-conditional mutant MET3-FBA1/fba1 shows strongly reduced enzyme expression
Y348F
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the mutant shows unaltered FBP aldolase activity, but has lost FBP phosphatase activity (less than 5%)
additional information
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isolation of thermostable variants of the class II fructose bisphosphate aldolase following four rounds of directed evolution using DNA shuffling of the fda gene. The variants show increased thermostability with no loss of catalytic function at room temperature
K325A
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decreased kcat
additional information
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isolation of thermostable variants of the class II fructose bisphosphate aldolase following four rounds of directed evolution using DNA shuffling of the fda gene. The variants show increased thermostability with no loss of catalytic function at room temperature
L256P
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tetramers dissociate into subunits with greatly impaired enzymatic activity
additional information
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chimeric enzymes between two human aldolases A, B, or C with different catalytic properties
K229M
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residual background activity
additional information
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AB_All mutant, isozyme-specific residues from aldolase B swapped into aldolase A and vice versa, decreased Km and kcat compared to aldolase A, similar Km and kcat to aldolase B
Y348F
Sulfolobus tokodaii 7
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the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 3.5fold lower than the wild-type value, the kcat/Km-value for the fructose-bisphosphate aldolase reaction of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) in the anabolic direction is 16fold lower than wild-type value
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additional information
Q55664
sll1330 deletion mutant
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
renaturation of acid-denatured enzyme
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enzyme does not refold into an enzymatically active conformation following denaturation
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
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inhibitors of class II Fba can be potential drugs against microorganisms
medicine
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mutations in aldolase B gene cause hereditary fructose intolerance, most common intolerance allele encodes a A149P substitution
medicine
P05062
aldolase B deficiency causes hereditary fructose intolerance
medicine
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potential drug target
medicine