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Gene Review:

ECs3796 - fructose-bisphosphate aldolase

Escherichia coli O157:H7 str. Sakai

Siebers, B. et al., Packman, L.C. et al., Izard, T. et al., Lee, J.H. et al., Cooper, S.J. et al., et al.

Siebers, Brinkmann, Dörr, Tjaden, Lilie, van der Oost, Verhees,

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Disease relevance of ECs3796

Comparison with the E. coli structure also indicates a structural basis for thermostability by Taq FBP aldolase [1].
Here we report the crystal structure of a metallo-dependent or class II FBP aldolase from an extreme thermophile, Thermus aquaticus (Taq) [1].
The autotrophic FBP aldolase proteins from X. flavus, Alcaligenes eutrophus, and Rhodobacter sphaeroides form a tight cluster, with the proteins from gram-positive bacteria as the closest relatives [2].
Phosphorylation (+ 80 Da), a known modification in an FBP-aldolase from Bacillus subtilis and a suspected modification in this E. coli aldolase, was ruled out as the extra mass was readily removed by treatment with dithiothreitol [3].

High impact information on ECs3796

Taq FBP aldolase subunits exhibit two distinct conformational states corresponding to loop regions that are in either open or closed position with respect to the active site [1].
As revealed by phylogenetic analyses, orthologs of the T. tenax and P. furiosus enzyme appear to be present in almost all sequenced archaeal genomes, as well as in some bacterial genomes, strongly suggesting that this new enzyme family represents the typical archaeal FBP aldolase [4].
The recombinant FBP aldolases show preferred substrate specificity for FBP in the catabolic direction and exhibit metal-independent Class I FBP aldolase activity via a Schiff-base mechanism [4].
It was recently established that fructose-1,6-bisphosphate (FBP) aldolase (FBA) and tagatose-1,6-bisphosphate (TBP) aldolase (TBA), two class II aldolases, are highly specific for the diastereoselective synthesis of FBP and TBP from glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP), respectively [5].
The amino acid sequence indicates the deletion of 4 residues from N-terminus, in comparison with the sequence of FBP-aldolase isozymes from other sources [6].

Biological context of ECs3796

The state of post-translational modification of the class-II fructose-1,6-bisphosphate aldolase (FBP-aldolase) purified from Escherichia coli was examined by electrospray ionisation mass spectrometry (ESI-MS) [3].
Fructose-1,6-bisphosphate aldolase (FBP-aldolase) is used in gluconeogenesis and glycolysis; the enzyme controls the condensation of dihydroxyacetone phosphate with glyceraldehyde-3-phosphate to yield fructose-1,6-bisphosphate [7].

References

Induced fit movements and metal cofactor selectivity of class II aldolases: structure of Thermus aquaticus fructose-1,6-bisphosphate aldolase. Izard, T., Sygusch, J. J. Biol. Chem. (2004) [Pubmed]
Primary structure and phylogeny of the Calvin cycle enzymes transketolase and fructosebisphosphate aldolase of Xanthobacter flavus. van den Bergh, E.R., Baker, S.C., Raggers, R.J., Terpstra, P., Woudstra, E.C., Dijkhuizen, L., Meijer, W.G. J. Bacteriol. (1996) [Pubmed]
A reactive, surface cysteine residue of the class-II fructose-1,6-bisphosphate aldolase of Escherichia coli revealed by electrospray ionisation mass spectrometry. Packman, L.C., Berry, A. Eur. J. Biochem. (1995) [Pubmed]
Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of archaeal type class I aldolase. Siebers, B., Brinkmann, H., Dörr, C., Tjaden, B., Lilie, H., van der Oost, J., Verhees, C.H. J. Biol. Chem. (2001) [Pubmed]
Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus. Lee, J.H., Bae, J., Kim, D., Choi, Y., Im, Y.J., Koh, S., Kim, J.S., Kim, M.K., Kang, G.B., Hong, S.I., Lee, D.S., Eom, S.H. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
Molecular evolution of amphioxus fructose-1,6-bisphosphate aldolase. Kuba, M., Yatsuki, H., Kusakabe, T., Takasaki, Y., Nikoh, N., Miyata, T., Yamaguchi, T., Hori, K. Arch. Biochem. Biophys. (1997) [Pubmed]
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. Cooper, S.J., Leonard, G.A., McSweeney, S.M., Thompson, A.W., Naismith, J.H., Qamar, S., Plater, A., Berry, A., Hunter, W.N. Structure (1996) [Pubmed]

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