Taxonomic distribution of proteins containing Aldolase_II domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing Aldolase_II domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Catalytic mechanism of the metal-dependent fuculose aldolase fromEscherichia coli as derived from the structure.

Dreyer MK, Schulz GE
J Mol Biol. 1996; 259: 458-66

The structure of L-fuculose-1-phosphate aldolase in a cubic crystal formhas been determined with and without the inhibitorphosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm)resolution, respectively. This inhibitor mimics the enediolate transitionstate of the substrate moiety dihydroxyacetone phosphate. The structuresshowed that dihydroxyacetone phosphate ligates the zinc ion of thismetal-dependent class II aldolase with its hydroxyl and keto oxygen atoms,shifting Glu73 away from the zinc coordination sphere to a non-polarenvironment. At this position Glu73 accepts a proton in the initialreaction step, producing the enediolate which is then stabilized by thezinc ion. The other substrate moiety L-lactaldehyde was modeled, becauseno binding structure is yet available.

The spatial structure of the class II L-fuculose-1-phosphate aldolase fromEscherichia coli.

Dreyer MK, Schulz GE
J Mol Biol. 1993; 231: 549-53

The three-dimensional structure of L-fuculose-1-phosphate aldolase (FucA)from Escherichia coli was determined by X-ray crystallography at aresolution of 2.13 A. The enzyme is a homotetramer with an M(r) of 23,775per subunit. Since its activity depends on the presence of metal ions(Zn2+) the enzyme belongs to the class II aldolases. As expected fromamino acid sequence comparisons, this first structure of a class IIaldolase shows no similarity to the known structures of class I aldolases.It has some unusual features concerning the overall chain fold, thequaternary structure, and the co-ordination of the catalytically activezinc ion. A sequence comparison with the data bank indicated that themiddle domain of the enzyme L-ribulose-5-phosphate-4-epimerase ishomologous to FucA and may contain an active-center metal ion.