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4.1.2.13: fructose-bisphosphate aldolase

This is an abbreviated version!
For detailed information about fructose-bisphosphate aldolase, go to the full flat file.

Word Map on EC 4.1.2.13

Reaction

D-fructose 1,6-bisphosphate
=
glycerone phosphate
 +
D-glyceraldehyde 3-phosphate

Synonyms

1,6-Diphosphofructose aldolase, 37 kDa major allergen, 41 kDa antigen, ALD, ALDC, aldoA, Aldob, aldolase, aldolase A, aldolase B, aldolase C, aldolase, fructose diphosphate, ALDP, bifunctional fructose-1,6-bisphosphate aldolase/phosphatase, Brain-type aldolase, Ca-FBA-II, CE1, CE2, class I Fba, class I fructose 1,6-bisphosphate aldolase, class I fructose bisphosphate aldolase, class I fructose-1,6-bisphosphate aldolase, class I muscle fructose bis-phosphate aldolase, class II aldolase, class II FBA, class II FBP aldolase, class II fructose 1,6-bisphosphate aldolase, class II fructose bisphosphate aldolase, class II fructose-1,6-bisphosphate aldolase, class IIa fructose 1,6-bisphosphate aldolase, class IIb fructose 1,6-bisphosphate aldolase, ClassII FBP-aldolase, CoFBA1, CoFBA2, CoFBA3, CoFBA4, D-fructose-1,6-bisphosphate aldolase, D-fructose-1,6-bisphosphate D-glyceraldehyde-3-P-lyase, D-fructose-6-phosphate aldolase, Diphosphofructose aldolase, DLF, EC 4.1.2.7, F1,6-P2 aldolase, F1,6P2 aldolase, F16BP aldolase, FBA, FBA class II, FBA-II, Fba1, Fba1p, Fba2, FBA7, FbaA, FbaB, FbaC, FBAld, FbaP, FBP aldolase, FBP aldolase/phosphatase, FBP-aldolase, FBPA, FBPA I, FBPA-1, FBPA/P, FDP aldolase, FPA, Fru-1,6-P2 aldolase, Fru-P2A, Fructoaldolase, fructose 1,6 bisphosphate aldolase, fructose 1,6-bisphosphatase/aldolase, Fructose 1,6-bisphosphate aldolase, fructose 1,6-bisphosphate aldolase/phosphatase, Fructose 1,6-diphosphate aldolase, Fructose 1-monophosphate aldolase, Fructose 1-phosphate aldolase, fructose bis-phosphate aldolase, Fructose bisphosphate aldolase, Fructose diphosphate aldolase, fructose-1,6-biphosphate aldolase, fructose-1,6-bisphosphate (FBP) aldolase/phosphatase, fructose-1,6-bisphosphate aldolase, fructose-1,6-bisphosphate aldolase A, fructose-1,6-bisphosphate aldolase B, fructose-1,6-bisphosphate aldolase class II, fructose-1,6-bisphosphate aldolase/phosphatase, fructose-1,6-bisphosphate muscle aldolase, Fructose-1,6-bisphosphate triosephosphate-lyase, fructose-bisphosphate aldolase, fructose-bisphosphate aldolase A, FSA, fuculose aldolase, heat-induced protein 44, HIP44, IgE-binding allergen, ketose 1-phosphate aldolase, Leishmania aldolase, Liver-type aldolase, MGA3_01355, MJ0400-His6, More, MtFBA, Muscle-type aldolase, Ov-fba-1, OvFBPA-1, Pcal_0111, Phosphofructoaldolase, SMALDO, SSO0286, STK_03180, TgALD1, Tneu_0133, TnFBPAP, Tt-FBPA, zerebrin II, zymohexase

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.13 fructose-bisphosphate aldolase

Crystallization

Crystallization on EC 4.1.2.13 - fructose-bisphosphate aldolase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.35 A resolution. Space group P212121, with unit-cell parameters a = 72.39, b = 127.71, c = 157.63 A. The structure shares the typical barrel tertiary structure and tetrameric quaternary structure reported for previous fructose bisphosphate aldolase structures and exhibits the same Schiff base in the active site
in the presence of the native substrate FBP, to 2.37 A resolution, and also with the partial substrate analog phosphate, to 2.0 A resolution. The structure shares the typical barrel tertiary structure reported for previous fructose bisphosphate aldolase structures and exhibits the same Schiff base in the active site. The quaternary structure is dimeric
class II aldolase in complex with phosphoglycolohydroxamate
crystals of recombinant fructose-1,6-bisphosphate aldolase class I are obtained by the sitting-drop vapour-diffusion technique in a condition consisting of 19 mg/ml FBPA I in 0.1 M Tris pH 9.0, 10% (w/v) polyethylene glycol 8000 and diffract to 2.0 A resolution. The crystals belong to the monoclinic space group C2, with unit-cell parameters 217.7 A (a), 114.9 A (b), 183.9 A (c), 124.6° (beta)
-
sitting drop vapor diffusion method, using 0.1 M Tris pH 9.0, 10% (w/v) polyethylene glycol 8000
-
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
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
-
comparative docking analysis shows that enzyme-substrate complex is forming similar Schiff base intermediate and conducts C3-C4 bond cleavage by forming hydrogen bonding with reaction catalyzing Glu191, reactive Lys150, and Schiff base forming Lys233. The noncovalent complex with inhibitor mannitol-1, 6 bisphosphate is forming cabinolamine precursor and the proton transfer by the formation of hydrogen bond between mannitol-1, 6 bisphosphate O2 with Glu191 enabling stabilization of cabinolamine transition state, which confirms the similar inhibition mechanism
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
in complex with inhibitor phosphoglycolohydroxamate as a mimic of the hydroxyenolate intermediate- and dihydroxyacetone phosphate-bound form of the enzyme, to 1.58 A resolution. Residue E169 facilitates a water-mediated deprotonation-protonation step of the reaction mechanism
native form and in complex with a hydroxamate substrate analog, to 2.35- and 1.9 A resolution, respectively. Inhibitor attachment has no effect on the plasminogen binding activity of the enzyme, it competes with the natural substrate, fructose 1,6-bisphosphate, and substantiates a reaction mechanism associated with metallodependent aldolases involving recruitment of the catalytic zinc ion by the substrate upon active site binding
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 Å 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
crystals are grown at 20°C by the hanging-drop vapour-diffusion method. Three-dimensional structures of the enzyme in a ligand-free state as well as in complex with the substrates glycerone phosphate and D-glyceraldehyde 3-phosphate and the product D-fructose 1,6-bisphosphate to resolutions up to 1.3?A
hanging drop vapor diffusion at 20°C. The final crystal condition is comprised of 1.6 M ammonium citrate pH 7.5 and is optimized with 3 M NDSB 195, yielding a 2.1 A data set in a P2(1)2(1)2 space group
hanging drop vapor diffusion method, using 1.6 M ammonium citrate (pH 7.5)
sitting-drop vapour-diffusion method at 25°C, 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
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
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
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
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
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