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Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Giardia intestinalis and UniProt Accession O97447

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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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Giardia intestinalis
UNIPROT: O97447
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Word Map
The taxonomic range for the selected organisms is: Giardia intestinalis
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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-
-
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37 kDa major allergen
-
-
-
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41 kDa antigen
-
-
-
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aldolase
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-
-
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aldolase, fructose diphosphate
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-
-
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ALDP
-
-
-
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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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Diphosphofructose aldolase
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-
-
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FBP aldolase
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-
-
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Fru-P2A
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-
-
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Fructoaldolase
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-
-
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Fructose 1,6-bisphosphate aldolase
Fructose 1,6-diphosphate aldolase
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-
-
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Fructose 1-monophosphate aldolase
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-
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Fructose 1-phosphate aldolase
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-
-
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Fructose bisphosphate aldolase
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-
-
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Fructose diphosphate aldolase
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-
-
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fructose-1,6-biphosphate aldolase
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Fructose-1,6-bisphosphate triosephosphate-lyase
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-
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IgE-binding allergen
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-
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ketose 1-phosphate aldolase
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-
-
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Liver-type aldolase
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-
-
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Muscle-type aldolase
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-
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Phosphofructoaldolase
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-
-
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SMALDO
-
-
-
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zymohexase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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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
-
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
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
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-
FBPA exhibits very low activity toward D-tagatose-1,6-bisphosphate
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
FBPA belongs to the class II zinc-dependent aldolase family, each subunit contains a Zn2+ cofactor
Zn2+
-
dependent, the active site contains a zinc ion
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-tagatose 1,6-bisphosphate
competitive inhibitor
([3-hydroxy-2-oxo-4-[(phosphonomethoxy)methyl]pyridin-1(2H)-yl]methyl)phosphonic acid
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([3-hydroxy-2-oxo-4-[2-(phosphonooxy)ethyl]pyridin-1(2H)-yl]methyl)phosphonic acid
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([3-hydroxy-4-[(1R)-1-hydroxy-2-(phosphonooxy)ethyl]-2-oxopyridin-1(2H)-yl]methyl)phosphonic acid
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([3-hydroxy-4-[(1S)-1-hydroxy-2-(phosphonooxy)ethyl]-2-oxopyridin-1(2H)-yl]methyl)phosphonic acid
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([4,5-dihydroxy-6-[2-(phosphonooxy)ethyl]pyridin-3-yl]methyl)phosphonic acid
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2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl dihydrogen phosphate
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2-hydroxy-2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl dihydrogen phosphate
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Phosphoglycolohydroxamate
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tagatose 1,6-bisphosphate
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[(3-hydroxy-2-oxopyridin-1(2H)-yl)methyl]phosphonic acid
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[2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl]phosphonic acid
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[[(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)methoxy]methyl]phosphonic acid
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[[3-hydroxy-2-oxo-4-(2-phosphonoethyl)pyridin-1(2H)-yl]methyl]phosphonic acid
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017 - 0.016
D-fructose 1,6-bisphosphate
0.0017 - 0.002
D-fructose 1,6-bisphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.63 - 3.55
D-fructose 1,6-bisphosphate
3.55
D-fructose 1,6-bisphosphate
-
at pH 7.5 and 25°C, in the absence of Zn2+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
40 - 2000
D-fructose 1,6-bisphosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11
([3-hydroxy-2-oxo-4-[(phosphonomethoxy)methyl]pyridin-1(2H)-yl]methyl)phosphonic acid
-
at pH 7.5 and 25°C
0.014
([3-hydroxy-2-oxo-4-[2-(phosphonooxy)ethyl]pyridin-1(2H)-yl]methyl)phosphonic acid
-
at pH 7.5 and 25°C
0.09
([3-hydroxy-4-[(1R)-1-hydroxy-2-(phosphonooxy)ethyl]-2-oxopyridin-1(2H)-yl]methyl)phosphonic acid
-
at pH 7.5 and 25°C
0.01
([3-hydroxy-4-[(1S)-1-hydroxy-2-(phosphonooxy)ethyl]-2-oxopyridin-1(2H)-yl]methyl)phosphonic acid
-
at pH 7.5 and 25°C
0.015
([4,5-dihydroxy-6-[2-(phosphonooxy)ethyl]pyridin-3-yl]methyl)phosphonic acid
-
at pH 7.5 and 25°C
0.9
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl dihydrogen phosphate
-
at pH 7.5 and 25°C
2.3
2-hydroxy-2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl dihydrogen phosphate
-
at pH 7.5 and 25°C
0.0024
Phosphoglycolohydroxamate
-
at pH 7.5 and 25°C, in the absence of Zn2+
0.001
tagatose 1,6-bisphosphate
-
at pH 7.5 and 25°C
1.2
[(3-hydroxy-2-oxopyridin-1(2H)-yl)methyl]phosphonic acid
-
at pH 7.5 and 25°C
0.81
[2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl]phosphonic acid
-
at pH 7.5 and 25°C
0.97
[[(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)methoxy]methyl]phosphonic acid
-
at pH 7.5 and 25°C
0.8
[[3-hydroxy-2-oxo-4-(2-phosphonoethyl)pyridin-1(2H)-yl]methyl]phosphonic acid
-
at pH 7.5 and 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O97447_GIAIN
323
0
35244
TrEMBL
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35380
-
calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
D83A and D255A mutant enzymes, hanging drop vapor diffusion method, using 18-25% (w/v) glycol 3350 and 0.2 M NH4NO3
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
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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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D255A
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Sepharose Q chromatography, Sephacryl 100 gel filtration, and phenyl-Sepharose chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21(DE3)Star
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Galkin, A.; Kulakova, L.; Melamud, E.; Li, L.; Wu, C.; Mariano, P.; Dunaway-Mariano, D.; Nash, T.E.; Herzberg, O.
Characterization, kinetics, and crystal structures of fructose-1,6-bisphosphate aldolase from the human parasite, Giardia lamblia
J. Biol. Chem.
282
4859-4867
2007
Giardia intestinalis
Manually annotated by BRENDA team
Galkin, A.; Li, Z.; Li, L.; Kulakova, L.; Pal, L.R.; Dunaway-Mariano, D.; Herzberg, O.
Structural insights into the substrate binding and stereoselectivity of Giardia fructose-1,6-bisphosphate aldolase
Biochemistry
48
3186-3196
2009
Giardia intestinalis (O97447), Giardia intestinalis
Manually annotated by BRENDA team
Li, Z.; Liu, Z.; Cho, D.W.; Zou, J.; Gong, M.; Breece, R.M.; Galkin, A.; Li, L.; Zhao, H.; Maestas, G.D.; Tierney, D.L.; Herzberg, O.; Dunaway-Mariano, D.; Mariano, P.S.
Rational design, synthesis and evaluation of first generation inhibitors of the Giardia lamblia fructose-1,6-biphosphate aldolase
J. Inorg. Biochem.
105
509-517
2011
Giardia intestinalis
Manually annotated by BRENDA team