fructose-1,6-bisphosphate triosephosphate-lyase
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase
Carbon fixation in photosynthetic organisms
HIS 110;GLU 174;HIS 226;HIS 264(Catalytic zinc);VAL 225;GLY 227;GLY 265;SER 267(Monovalent metal)
HIS 110;GLU 174; ;HIS 264(Catalytic zinc);VAL 225; ;GLY 265;SER 267(Monovalent metal)
Magnetic resonance studies of the role of the divalent cation in the mechanism of yeast aldolase.
18O studies of the mechanisms of yeast and muscle aldolases.
Initiating a crystallographic study of a class II fructose-1,6-bisphosphate aldolase.
Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli.
Properties of fructose-1,6-bisphosphate aldolase from Escherichia coli: an NMR analysis.
Functional characterization of an extreme thermophilic class II fructose-1,6-bisphosphate aldolase.
Some recent developments in the preparation of novel recognition systems: a recognition site for the selective catalysis of an aldol condensation using molecular imprinting and specific affinity motifs for alpha-chymotrypsin using a phage display peptide library.
Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase.
Identification of arginine 331 as an important active site residue in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli.
The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold.
Epimerization via carbon-carbon bond cleavage. L-ribulose-5-phosphate 4-epimerase as a masked class II aldolase.
The crystal structure of Escherichia coli class II fructose-1, 6-bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals details of mechanism and specificity.
Conserved residues in the mechanism of the E. coli Class II FBP-aldolase.
Exploring substrate binding and discrimination in fructose1, 6-bisphosphate and tagatose 1,6-bisphosphate aldolases.
Crystallization and preliminary X-ray analysis of native and selenomethionine fructose-1,6-bisphosphate aldolase from Thermus aquaticus.
Brownian dynamics simulations of aldolase binding glyceraldehyde 3-phosphate dehydrogenase and the possibility of substrate channeling.
Molecular cloning, expression, purification, and characterization of fructose-1,6-bisphosphate aldolase from Thermus aquaticus.
A functional role for a flexible loop containing Glu182 in the class II fructose-1,6-bisphosphate aldolase from Escherichia coli.
The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase.
Although Glu174 is bound to the catalytic zinc ion, it moves away from the zinc ion to allow the substrate/product (Glycerone phosphate; GP) moiety to coordinate the ion during the catalysis (see [10]). Here, zinc ion functions as a Lewis acid electron sink, and polarizes the carbonyl bond of GP, for the elimination or addition reaction. A monovalent cation is required for substrate binding, although it is not involved in catalysis. According to the literature [18], although Glu182 is distant from the active site in the absence of substrate, it would be brought into a position to act as a general base on binding of substrates. This enzyme catalyzes two reverse reactions, which are composed of two reactions respectively (see [12]): (#1) the aldol condensation of a ketose, Glycerone phosphate (GP) and an aldose, glyceraldehyde 3-phosphate (G3P) to form the acyclic form of fructose 1,6-bisphospahte (FBP); that is addition of GP to the double-bond (carbonyl group) of G3P. (In Gluconeogenesis pathway) (A) Isomerization: (B) Addition of GP to the double-bond (carbonyl group) of G3P: (#2) the clevage of FBP into GP and G3P; that is elimination of GP from FBP to form a new double-bond in another product, G3P. (In glycolysis pathway) (C) Elimination of GP: (D) Isomerization: These catalytic reactions proceeds as follows (see [12] & [18]): (A) Isomerization: (A1) Carbonyl group and hydroxyl group of GP are bound to the catalytic zinc ion, replacing Glu174. Here, the zinc ion polarizes the carbonyl bond of the ketose substrate, GP, which increases the acidity of the hydroxymethylene (C1) hydrogen atoms, facilitating the next reaction, deprotonation. (A2) Glu182 acts as a general base to deprotonate the C1 atom, leading to the formation of ene-diolate (carbanion) intermediate. This intermediate is stabilized by Asn286. (B) Addition of the ene-diolate intermediate to the double-bond (carbonyl group) of G3P (B1) The second substrate (aldehyde), G3P, which is electrophilic, binds to the active site, to interact with the nucleophilic ene-diolate intermediate. (The two planes of the ene-diolate nucleophile and the carbonyl acceptor must be nearly parallel for the C-C bond formation.) Here, Asp109 polarizes the addition site, the C1 carbonyl group of G3P (as a modulator). (B2) The C1 atom of the ene-diolate intermediate makes a nucleophilic attack on the C1 carbonyl carbon of G3P, forming C-C bond. Here, Asp109 protonate the carbonyl oxygen of G3P, leading to formation of the hydroxyl group. At the same time, a carbonyl group is formed at the C2 carbon of the product, FBP. On the other hand, the reverse reaction (C) proceeds as follows: (C) Elimination of GP from FBP to form a new double-bond in G3P (C1) The carbonyl oxygen (O2) and C3 hydroxyl group of FBP are bound to the catalytic zinc ion. This zinc ion polarizes the carbonyl bond of FBP. (C2) Asp109 acts as a general base to deprotonate the C4 hydroxyl group of FBP (deprotonation site of leaving group), leading to the C-C bond cleavage. This cleavage gives the ene-diolate intermediate, which is bound to the catalytic zinc ion, and a leaving product, G3P. The ene-diolate intermediate is stabilized by Asn286. (C3) G3P is released from the active site. (D) Isomerization: (D1) Glu182 acts as a general acid to protonate the C1 sp2 carbon of the intermediate, to form the carbonyl group at the C2 carbon.