Structural highlights
Function
[ALF_ECOLI] Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The molecular architecture of the Class II E. coli fructose 1,6-bisphosphate aldolase dimer was determined to 1.6 A resolution. The subunit fold corresponds to a singly wound alpha/beta-barrel with an active site located on the beta-barrel carboxyl side of each subunit. In each subunit there are two mutually exclusive zinc metal ion binding sites, 3.2 A apart; the exclusivity is mediated by a conformational transition involving side-chain rotations by chelating histidine residues. A binding site for K+ and NH4+ activators was found near the beta-barrel centre. Although Class I and Class II aldolases catalyse identical reactions, their active sites do not share common amino acid residues, are structurally dissimilar, and from sequence comparisons appear to be evolutionary distinct.
Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase.,Blom NS, Tetreault S, Coulombe R, Sygusch J Nat Struct Biol. 1996 Oct;3(10):856-62. PMID:8836102[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zgiby SM, Thomson GJ, Qamar S, Berry A. Exploring substrate binding and discrimination in fructose1, 6-bisphosphate and tagatose 1,6-bisphosphate aldolases. Eur J Biochem. 2000 Mar;267(6):1858-68. PMID:10712619
- ↑ Blom NS, Tetreault S, Coulombe R, Sygusch J. Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase. Nat Struct Biol. 1996 Oct;3(10):856-62. PMID:8836102
