fructose-1,6-bisphosphate triosephosphate-lyase
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase
Carbon fixation in photosynthetic organisms
Alternative binding of two sequential glycolytic enzymes to microtubules. Molecular studies in the phosphofructokinase/aldolase/microtubule system.
Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase.
18O studies of the mechanisms of yeast and muscle aldolases.
Proton exchange of the pro-S hydrogen at C-1 in dihydroxyacetone phosphate, D-fructose 1,6-bisphosphate and D-fructose 1-phosphate catalysed by rabbit-muscle aldolase.
Affinity labeling of a previously undetected essential lysyl residue in class I fructose bisphosphate aldolase.
Rabbit muscle aldolase catalyzed proton exchange of hydroxyacetone phosphate with solvent.
Interaction of the aldolase and the membrane of human erythrocytes.
Changes associated with glycolytic-enzyme binding in the equatorial X-ray-diffraction pattern of glycerinated rabbit psoas muscle.
Identification of the C-1-phosphate-binding arginine residue of rabbit-muscle aldolase. Isolation of 1,2-cyclohexanedione-labeled peptide by chemisorption chromatography.
Changes in activity of fructose-1,6-bisphosphate aldolase in livers of fasted rabbits and accumulation of crossreacting immune material.
Membrane-bound fructose 1,6-bisphosphate aldolase: catalytic activity and mechanisms of desorption.
The low-resolution structure of human muscle aldolase.
Chemistry of proton abstraction by glycolytic enzymes (aldolase, isomerases and pyruvate kinase).
A 1H n.m.r. study of isotope exchange catalysed by glycolytic enzymes in the human erythrocyte.
Fructose-1,6-bisphosphate-aldolase from rabbit muscle. Half of the sites reactivity at low temperature.
Mechanism of aldolase binding to erythrocyte membrane: Part II. Kinetic aspects.
Interaction of the dissociable glycerol-3-phosphate dehydrogenase and fructose-1,6-bisphosphate aldolase. Quantitative analysis by an extrinsic fluorescence probe.
Fructose-1,6-bisphosphate aldolase from rabbit muscle: different catalytic behavior of the dihydroxyacetone phosphate binding sites at low temperature.
Extreme X-ray sensitive modification of type I aldolases by blue dye ligand chromatography.
Characterization and comparison of soluble and immobilized pig muscle aldolases.
Structure of rabbit muscle aldolase at low resolution.
Specific, limited tryptic modification of wheat-germ fructose-bisphosphate aldolase subunits: destruction of catalytic activity but not of ability to establish precise subunit-subunit recognition.
A simple approach to detect active-site-directed enzyme-enzyme interactions. The aldolase/glycerol-phosphate-dehydrogenase enzyme system.
Human aldolase A deficiency associated with a hemolytic anemia: thermolabile aldolase due to a single base mutation.
Immobilization of pig muscle aldolase on a silica-based support.
The crystal structure of human muscle aldolase at 3.0 A resolution.
Human aldolase A of a hemolytic anemia patient with Asp-128----Gly substitution: characteristics of an enzyme generated in E. coli transfected with the expression plasmid pHAAD128G.
Topography and conformational changes of fructose-1,6-bisphosphate aldolase.
The crystal structure of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster at 2.5 A resolution.
Carboxyl terminus region modulates catalytic activity of recombinant maize aldolase.
Activity and specificity of human aldolases.
Metabolite channeling versus free diffusion: reinterpretation of aldolase-catalysed inactivation of glyceraldehyde-3-phosphate dehydrogenase.
Aldolase-catalyzed diketone phosphate formation from oxoaldehydes. NMR studies and metabolic significance.
Paracatalytic self-inactivation of fructose-1,6-bisphosphate aldolase. Structure of the crosslink formed at the active site.
A data-based reaction mechanism for type I fructose bisphosphate aldolase.
Lysine-146 of rabbit muscle aldolase is essential for cleavage and condensation of the C3-C4 bond of fructose 1,6-bis(phosphate).
Solution structure of a band 3 peptide inhibitor bound to aldolase: a proposed mechanism for regulating binding by tyrosine phosphorylation.
The molecular nature of the F-actin binding activity of aldolase revealed with site-directed mutants.
Disruption of the aldolase A tetramer into catalytically active monomers.
Crystallisation and Preliminary X-Ray Diffraction Studies on Human Liver Aldolase.
Immune versus natural selection: antibody aldolases with enzymic rates but broader scope.
Crystal structure of fructose-1,6-bisphosphate aldolase from the human malaria parasite Plasmodium falciparum.
Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3 A(,).
Mechanism of metabolite transfer in coupled two-enzyme reactions involving aldolase.
Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications.
Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at arginine 303 in human liver aldolase.
Expression, purification, and characterization of natural mutants of human aldolase B. Role of quaternary structure in catalysis.
Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases.
Chemoenzymatic synthesis of the microbial elicitor (-)-syringolide via a fructose 1,6-diphosphate aldolase-catalyzed condensation reaction.
The structure of human liver fructose-1,6-bisphosphate aldolase.
Snapshots of catalysis: the structure of fructose-1,6-(bis)phosphate aldolase covalently bound to the substrate dihydroxyacetone phosphate.
Brownian dynamics simulations of aldolase binding glyceraldehyde 3-phosphate dehydrogenase and the possibility of substrate channeling.
Structural and functional analysis of aldolase B mutants related to hereditary fructose intolerance.
A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases.
Docking multiple conformations of a flexible ligand into a protein binding site using NMR restraints.
Presteady-state kinetic evidence for a ring-opening activity in fructose-1,6-(bis)phosphate aldolase.
This enzyme is class I aldolase. The class II aldolase (S00235 in EzCatDB) has got totally different mechanism with zinc ion at the active site. The literature [51] & [54] indicate different catalytic residues. Accoridng to the literature [51], Glu187 plays a catalytic role by protonating the C2-hydroxyl group during Schiff-base formation, and Asp33 is involved in C3-C4 bond cleavage. In contrast, Glu187 is involved in the bond cleavage, according to the literature [54]. (The active site structures support the literature [54].) According to the literature [51], [54] & [56], the catalytic reaction of this enzyme may proceeds as follows; (A) Eliminative double-bond formation; Ring-opening/hemiketal cleavage (B) Exchange of double-bonded atoms; Schiff-base formation (B1) Glu187 acts as a general base to abstract a proton from the sidechain of Lys229, enhancing its nucleophilicity (see [54]). Here, the function of Glu187 is modulated by Glu189. (B2) The activated Lys229 makes a nucleophilic attack on C2-carbonyl group, to form a carbinolamine intermediate. (Here, a proton must transfer from the sidechain amine of Lys229 to the C2-carbonyl oxygen, with a probable assistance by Glu187. Glu187 may protonate the C2-carbonyl oxygen, and then deprotonate the amine of Lys229.) (B3) The lone pair of Lys229 makes another attak on C2-carbon, whilst Glu187 acts as a general acid to protonate the eliminated hydroxyl group. This reaction leads to Schiff-base intermeidate formation. (C) Eliminative double-bond formation;C3-C4 bond cleavage (C1) Glu187 acts as a general base to deprotonate C4-hydroxyl group, leading to the C3-C4 bond cleavage (see [54]). Here, the electron sink (Schiff-base) formed at C2 facilitate the deprotonation, and formation of C2=C3 double-bond, or ketamine (or enamine) intermediate. (According to the literature [1], instead of Glu187, Asp33 acts as the base.) (C2) The first product, G3P, is released from the active site. (D) Isomerization; Shift of double-bond (D1) The lone pair at nitrogen atom of Lys229 makes an attack on C2 carbon, to form Schiff-base again, which leads to C3-carbanion intermediate. The carbanion seems to be stabilized by the protonated sidechain of Lys146. (D2) Asp33 protonates the carbanion, to form an imine intermediate. (E) Exchange of double-bonded atoms; Schiff-base deformation (E1) Glu187 acts as a general base, to activate a water molecule. (E2) The activated water makes a nucleophilic attack on the C2 carbon, to form a carbinolamine intermeidate. (Here, a proton must transfer from the hydroxyl group to the sidechain amine of Lys229, with a probable assistance by Glu187. Glu187 may protonate the sidechain of Lys229, and then deprotonate the hydroxyl group.) (E3) The lone pair at the hydroxyl group of carbinolamine makes a nucleophilic attack on the C2 carbon again, to release the sidechain of Lys229. (E4) Unprotonated Lys229 must be protonated by Glu187.