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Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Toxoplasma gondii and UniProt Accession B9PW35

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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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Toxoplasma gondii
UNIPROT: B9PW35
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The taxonomic range for the selected organisms is: Toxoplasma gondii
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
fructose-1,6-bisphosphate aldolase
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1,6-Diphosphofructose aldolase
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37 kDa major allergen
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-
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41 kDa antigen
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-
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aldolase
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aldolase, fructose diphosphate
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-
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ALDP
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-
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Brain-type aldolase
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-
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CE1
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-
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CE2
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class I fructose-1,6-bisphosphate aldolase
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Diphosphofructose aldolase
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FBP aldolase
Fru-P2A
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Fructoaldolase
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Fructose 1,6-bisphosphate aldolase
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Fructose 1,6-diphosphate aldolase
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Fructose 1-monophosphate aldolase
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Fructose 1-phosphate aldolase
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Fructose bisphosphate aldolase
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Fructose diphosphate aldolase
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fructose-1,6-bisphosphate aldolase
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Fructose-1,6-bisphosphate triosephosphate-lyase
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IgE-binding allergen
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ketose 1-phosphate aldolase
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Liver-type aldolase
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-
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Muscle-type aldolase
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Phosphofructoaldolase
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SMALDO
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-
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zymohexase
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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-
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-
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
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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
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
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-
-
?
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
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?, r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tagatose 1,6-bisphosphate
competitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00405 - 0.0045
D-fructose 1,6-bisphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.09
D-fructose 1,6-bisphosphate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
during invasion of the apicomplexan parasite Toxoplasma gondii into host cells, the enzyme serves in the role of a structural bridging protein, as opposed to its normal enzymatic role in the glycolysis pathway
metabolism
the enzyme is involved in glycolysis
physiological function
glycolytic enzyme
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized in the presence of glycerol and PEG 4000 at 4°C, producing crystals that are cryoprotected with a cryosolution containing reservoir and glycerol at a final concentration of 35% (v/v) before flash-cooling in liquid nitrogen. Crystallized in space group P22(1)2(1), with the biologically relevant tetramer in the asymmetric unit, and the structure has been determined via molecular replacement to a resolution of 2.0 A
sitting drop vapor diffusion method, using 0.1 M MOPS/HEPES-Na pH 7.9, 0.02 M sodium formate, 0.02 M ammonium acetate, 0.02 M trisodium citrate, 0.02 M sodium potassium L-tartrate, 0.02 M sodium oxamate, 0.02 M ammonium acetate, 12.5% (v/v) glycerol, 25% (w/v) PEG 4000
crystals are grown at 20°C by hanging-drop vapor diffusion using a 1:1 mixture of protein/precipitant. The enzyme crystallizes with one tetrameric subunit in the asymmetric unit of space group P4(2)2(1)2, adopting the classic (alpha/beta)8-barrel fold
hanging drop vapor diffusion method, using 0.1 M sodium acetate, pH 5.5, 0.2 M lithium sulfate, 3.5% (w/v) PEG 8000, and 10% (w/v) PEG 1000
the enzyme crystallizes with one molecule in the asymmetric unit and adopts an alpha8/beta8 TIM barrel fold classically associated with members of the aldolase family
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Co-TALON column chromatography and Superdex 200 gel filtration
HisTrap column chromatography and Superdex gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21-Star (DE3) cells
expression in Escherichia coli
expression in Escherichia coli BL21
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
constitutively expressed at steady state levels in all developmental stages
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boucher, L.E.; Bosch, J.
Structure of Toxoplasma gondii fructose-1,6-bisphosphate aldolase
Acta Crystallogr. Sect. F
70
1186-1192
2014
Toxoplasma gondii (B9PW35), Toxoplasma gondii, Toxoplasma gondii ATCC 50861 (B9PW35)
Manually annotated by BRENDA team
Heron, P.W.; Sygusch, J.
Isomer activation controls stereospecificity of class I fructose-1,6-bisphosphate aldolases
J. Biol. Chem.
292
19849-19860
2017
Toxoplasma gondii (Q8I8I2)
Manually annotated by BRENDA team
Tonkin, M.L.; Halavaty, A.S.; Ramaswamy, R.; Ruan, J.; Igarashi, M.; Ngo, H.M.; Boulanger, M.J.
Structural and functional divergence of the aldolase fold in Toxoplasma gondii
J. Mol. Biol.
427
840-852
2015
Toxoplasma gondii (A0A125YGE6), Toxoplasma gondii, Toxoplasma gondii ATCC 50611 (A0A125YGE6)
Manually annotated by BRENDA team