fructose-1,6-bisphosphate triosephosphate-lyase
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase
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.
Carbon fixation in photosynthetic organisms
18O studies of the mechanisms of yeast and muscle aldolases.
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.
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.
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.
Affinity labeling of a previously undetected essential lysyl residue in class I fructose bisphosphate aldolase.
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.
Alternative binding of two sequential glycolytic enzymes to microtubules. Molecular studies in the phosphofructokinase/aldolase/microtubule system.
Rabbit muscle aldolase catalyzed proton exchange of hydroxyacetone phosphate with solvent.
Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate 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.
Interaction of the aldolase and the membrane of human erythrocytes.
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.
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.
Presteady-state kinetic evidence for a ring-opening activity in fructose-1,6-(bis)phosphate aldolase.
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.
Brownian dynamics simulations of aldolase binding glyceraldehyde 3-phosphate dehydrogenase and the possibility of substrate channeling.
Docking multiple conformations of a flexible ligand into a protein binding site using NMR restraints.