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Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Homo sapiens and UniProt Accession P05062

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.13 fructose-bisphosphate aldolase
IUBMB Comments
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.
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Homo sapiens
UNIPROT: P05062
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
aldolase, aldolase a, aldolase b, aldolase c, aldoa, fructose-1,6-bisphosphate aldolase, fructose-bisphosphate aldolase, aldob, fructose bisphosphate aldolase, fructose 1,6-bisphosphate aldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldolase B
-
1,6-Diphosphofructose aldolase
-
-
-
-
37 kDa major allergen
-
-
-
-
41 kDa antigen
-
-
-
-
ALDC
-
-
aldoA
aldolase
-
-
-
-
aldolase C
aldolase, fructose diphosphate
-
-
-
-
ALDP
-
-
-
-
Brain-type aldolase
-
-
-
-
CE1
-
-
-
-
CE2
-
-
-
-
Diphosphofructose aldolase
-
-
-
-
FBP aldolase
-
-
-
-
Fru-1,6-P2 aldolase
-
-
Fru-P2A
-
-
-
-
Fructoaldolase
-
-
-
-
Fructose 1,6-bisphosphate aldolase
Fructose 1,6-diphosphate aldolase
-
-
-
-
Fructose 1-monophosphate aldolase
-
-
-
-
Fructose 1-phosphate aldolase
-
-
-
-
Fructose bisphosphate aldolase
-
-
-
-
Fructose diphosphate aldolase
-
-
-
-
fructose-1,6-bisphosphate aldolase A
-
-
Fructose-1,6-bisphosphate triosephosphate-lyase
-
-
-
-
fructose-bisphosphate aldolase A
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IgE-binding allergen
-
-
-
-
ketose 1-phosphate aldolase
-
-
-
-
Liver-type aldolase
-
-
-
-
Muscle-type aldolase
-
-
-
-
Phosphofructoaldolase
-
-
-
-
SMALDO
-
-
-
-
zerebrin II
-
-
zymohexase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-52-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
r
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
D-Xylulose 1-phosphate
?
show the reaction diagram
-
110% of the activity with fructose 1,6-diphosphate
-
-
?
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
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
-
ascorbic acid
-
-
ATP
-
-
erythrose 4-phosphate
-
-
fructose 6-phosphate
-
-
glucose 1-phosphate
-
-
glucose 6-phosphate
-
-
Glycerol 2,3-diphosphate
-
-
glyoxylate
-
-
IMP
-
-
ribose 5-phosphate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0023 - 0.032
D-fructose 1,6-bisphosphate
0.0017 - 0.05
D-Fructose 1-phosphate
0.0016 - 0.33
D-fructose 1,6-bisphosphate
0.0024 - 16.4
D-Fructose 1-phosphate
0.0016
D-Xylulose 1-phosphate
-
-
1.1 - 27
fructose 1-phosphate
additional information
additional information
-
Km-values of chimeric enzymes between two human aldolases A, B, or C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 6.08
D-fructose 1,6-bisphosphate
0.059 - 6.08
D-Fructose 1-phosphate
0.011 - 59.7
D-fructose 1,6-bisphosphate
0.008 - 2.8
D-Fructose 1-phosphate
0.75 - 10.8
fructose 1-phosphate
additional information
additional information
-
turnover-numbers of chimeric enzymes between two human aldolases A, B, or C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.13
N334K mutant, D-fructose 1-phosphate as substrate
0.28
N334K mutant, D-fructose 1,6-bisphosphate as substrate
0.38
W147R mutant, D-fructose 1-phosphate as substrate
0.58
L256P mutant, D-fructose 1-phosphate as substrate
0.64
W147R mutant, D-fructose 1,6-bisphosphate as substrate
0.81
L256P mutant, D-fructose 1,6-bisphosphate as substrate
0.86
Q354E mutant, D-fructose 1,6-bisphosphate as substrate
0.88
Q354E mutant, D-fructose 1-phosphate as substrate
0.94
wild-type enzyme, D-fructose 1-phosphate as substrate
0.97
wild-type enzyme, D-fructose 1,6-bisphosphate as substrate
15.7
mutant enzyme E206K
22.3
wild-type enzyme
6.1
mutant enzyme G346S
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 12
-
pH 4: about 80% of maximal activity, pH 12: about 75% of maximal activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15
-
gradual loss of activity above, enzyme from patients with fructose intolerance
40
-
wild-type enzyme, activity is stable up to 40°C, declines sharply above 40°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
the enzyme is a sensor of glucose availability that regulates AMP-activated protein kinase
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALDOB_HUMAN
364
0
39473
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
170000
tetrameric form, gel filtration
120000
-
liver enzyme, gel filtration
158000
170000
38000
-
4 * 38000, recombinant aldolase A and liver enzyme, SDS-PAGE
40000
-
4 * 40000, SDS-PAGE, equilibrium sedimentation in 6 M guanidine/HCl, SDS-PAGE
40000 - 60000
-
gel filtration, monomeric form, A149P, N334K, L256P, A337V mutant
57000
-
sucrose density gradient centrifugation, 30°C
71000
-
sucrose density gradient centrifugation, 4°C
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer
-
A149P and N334K mutants exist as mixture of protein conformers that encompass all molecular sizes between tetramer and monomer
tetramer
trimer
-
A149P and N334K mutants exist as mixture of protein conformers that encompass all molecular sizes between tetramer and monomer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A149P
no catalytic activity
L256P
melting temperature is 40°C versus 47°C for the wild-type enzyme
N334K
increased Km value
Q354E
kinetis resemble that of the wild-type enzyme
W147R
melting temperature is 40°C versus 47°C for the wild-type enzyme
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 25°C
C289A
-
activity similar to wild-type enzyme, more stable in long-term storage at 25°C
C338A
-
activity similar to wild-type enzyme, more stable in long-term storage at 25°C
C72A
-
activity similar to wild-type enzyme, more stable in long-term storage at 25°C
D34S
-
catalytically inactive mutant which still binds to D-fructose 1,6-bisphosphate
E206K
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
mutant enzyme has the same KM-value as the wild-type enzyme, but a 4fold lower turnover-number
L256P
-
tetramers dissociate into subunits with greatly impaired enzymatic activity
N334K
-
tetramers dissociate into subunits with greatly impaired enzymatic activity
R303W
-
retained tetrameric structure, altered kinetic properties
W147R
-
retained tetrameric structure, altered kinetic properties
Y363S
-
Y363S has reduced catalytic activity towards D-fructose 1,6-bisphosphate and fructose 1-phosphate
additional information
-
chimeric enzymes between two human aldolases A, B, or C with different catalytic properties
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
W147R melting temperature of W147R mutant and L256P mutant is 40°C versus 47°C for the wild-type enzyme
47
melting temperature of the wild-type enzyme
10
-
enzyme from patients with fructose intolerance shows increased temperature sensitivity, activity at 10°C is 6fold lower than that of the wild-type, and activity decreases substantially at higher temperatures
48
melting temperature of mutant E206K
54
melting temperature of wild-type enzyme is 54.4°C
55
melting temperature of mutant enzyme G346S is 54.8°C
60
-
30 min, about 90% loss of aldolase A activity with D-fructose 1,6-bisphosphate as substrate
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, wild-type and Q354E mutant: stable in 50% glycerol for 1 month, W147R and L256P mutant enzyme: aggregate after 15 days suggesting structural instability
-20°C, 50% v/v glycerol/20 mM TrisHCl, stable for at least 1 month
4°C, 20 mM Tris/HCl, pH 7.4, stable for at least 2 weeks
wild-type enzyme: 50% loss of activity after 3 months, mutants: accelerated loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
95% homogeneity
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ALDOA expression is upregulated under hypoxic conditions
enzyme expression is upregulated under hypoxic conditions
on stimulation with epidermal growth factor, the wound recovery area and ALDOA and its mRNA levels increase
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
aldolase B deficiency causes hereditary fructose intolerance
diagnostics
for patients with colorectal cancer mRNA expression is a significant prognostic factor for disease-free survival and for overall survival
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yeltman, D.R.; Harris, B.G.
Purification and characterization of aldolase from human erythrocytes
Biochim. Biophys. Acta
484
188-198
1977
Homo sapiens
Manually annotated by BRENDA team
Yeltman, D.R.; Harris, B.G.
Fructose-bisphosphate aldolase from human erythrocytes
Methods Enzymol.
90
251-254
1982
Homo sapiens
Manually annotated by BRENDA team
Bais, R.; James, H.M.; Rofe, A.M.; Conyers, A.J.
The purification and properties of human liver ketohexokinase. A role for ketohexokinase and fructose-bisphosphate aldolase in the metabolic production of oxalate from xylitol
Biochem. J.
230
53-60
1985
Homo sapiens
Manually annotated by BRENDA team
Kusakabe, T.; Motoki, K.; Hori, K.
Human aldolase C: characterization of the recombinant enzyme expressed in Escherichia coli
J. Biochem.
115
1172-1177
1994
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Doyle, S.A.; Tolan, D.R.
Characterization of recombinant human aldolase B and purification by metal chelate chromatography
Biochem. Biophys. Res. Commun.
206
902-908
1995
Homo sapiens
Manually annotated by BRENDA team
Kusakabe, T.; Motoki, K.; Sugimoto, Y.; Takasaki, Y.; Hori, K.
Human aldolase B: liver-specific properties of the isoenzyme depend on type B isozyme group-specific sequences
Protein Eng.
7
1387-1393
1994
Homo sapiens
Manually annotated by BRENDA team
Dalby, A.; Dauter, Z.; Littlechild, J.A.
Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications
Protein Sci.
8
291-297
1999
Homo sapiens
Manually annotated by BRENDA team
Dalby, A.R.; Tolan, D.R.; Littlechild, J.A.
The structure of human liver fructose-1,6-bisphosphate aldolase
Acta Crystallogr. Sect. D
57
1526-1533
2001
Homo sapiens
Manually annotated by BRENDA team
Malay, A.D.; Procious, S.L.; Tolan, D.R.
The temperature dependence of activity and structure for the most prevalent mutant aldolase B associated with hereditary fructose intolerance
Arch. Biochem. Biophys.
408
295-304
2002
Homo sapiens
Manually annotated by BRENDA team
Choi, K.H.; Shi, J.; Hopkins, C.E.; Tolan, D.R.; Allen, K.N.
Snapshots of catalysis: the structure of fructose-1,6-(bis)phosphate aldolase covalently bound to the substrate dihydroxyacetone phosphate
Biochemistry
40
13868-13875
2001
Homo sapiens
Manually annotated by BRENDA team
Esposito, G.; Vitagliano, L.; Santamaria, R.; Viola, A.; Zagari, A.; Salvatore, F.
Structural and functional analysis of aldolase B mutants related to hereditary fructose intolerance
FEBS Lett.
531
152-156
2002
Homo sapiens (P05062), Homo sapiens
Manually annotated by BRENDA team
Choi, K.H.; Tolan, D.R.
Presteady-state kinetic evidence for a ring-opening activity in fructose-1,6-(bis)phosphate aldolase
J. Am. Chem. Soc.
126
3402-3403
2004
Homo sapiens
Manually annotated by BRENDA team
Rellos, P.; Sygusch, J.; Cox, T.M.
Expression, purification, and characterization of natural mutants of human aldolase B. Role of quaternary structure in catalysis
J. Biol. Chem.
275
1145-1151
2000
Homo sapiens
Manually annotated by BRENDA team
Esposito, G.; Vitagliano, L.; Costanzo, P.; Borrelli, L.; Barone, R.; Pavone, L.; Izzo, P.; Zagari, A.; Salvatore, F.
Human aldolase A natural mutants: relationship between flexibility of the C-terminal region and enzyme function
Biochem. J.
380
51-56
2004
Homo sapiens (P04075), Homo sapiens
Manually annotated by BRENDA team
Arakaki, T.L.; Pezza, J.A.; Cronin, M.A.; Hopkins, C.E.; Zimmer, D.B.; Tolan, D.R.; Allen, K.N.
Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking isozyme structure with function
Protein Sci.
13
3077-3084
2004
Homo sapiens
Manually annotated by BRENDA team
Linke, S.; Goertz, P.; Baader, S.L.; Gieselmann, V.; Siebler, M.; Junghans, U.; Kappler, J.
Aldolase C/zebrin II is released to the extracellular space after stroke and inhibits the network activity of cortical neurons
Neurochem. Res.
31
1297-1303
2006
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Tochio, T.; Tanaka, H.; Nakata, S.; Hosoya, H.
Fructose-1,6-bisphosphate aldolase A is involved in HaCaT cell migration by inducing lamellipodia formation
J. Dermatol. Sci.
58
123-129
2010
Homo sapiens
Manually annotated by BRENDA team
Kawai, K.; Uemura, M.; Munakata, K.; Takahashi, H.; Haraguchi, N.; Nishimura, J.; Hata, T.; Matsuda, C.; Ikenaga, M.; Murata, K.; Mizushima, T.; Yamamoto, H.; Doki, Y.; Mori, M.
Fructose-bisphosphate aldolase A is a key regulator of hypoxic adaptation in colorectal cancer cells and involved in treatment resistance and poor prognosis
Int. J. Oncol.
50
525-534
2017
Homo sapiens (P04075), Homo sapiens
Manually annotated by BRENDA team
Zhang, C.S.; Hawley, S.A.; Zong, Y.; Li, M.; Wang, Z.; Gray, A.; Ma, T.; Cui, J.; Feng, J.W.; Zhu, M.; Wu, Y.Q.; Li, T.Y.; Ye, Z.; Lin, S.Y.; Yin, H.; Piao, H.L.; Hardie, D.G.; Lin, S.C.
Fructose-1,6-bisphosphate and aldolase mediate glucose sensing by AMPK
Nature
548
112-116
2017
Homo sapiens, Mus musculus
Manually annotated by BRENDA team