|PROSITE documentation PDOC00523|
Fructose-bisphosphate aldolase (EC 18.104.22.168) [1,2] is a glycolytic enzyme that catalyzes the reversible aldol cleavage or condensation of fructose-1,6-bisphosphate into dihydroxyacetone-phosphate and glyceraldehyde 3-phosphate. There are two classes of fructose-bisphosphate aldolases with different catalytic mechanisms. Class-II aldolases , mainly found in prokaryotes and fungi, are homodimeric enzymes which require a divalent metal ion - generally zinc - for their activity.
This family also includes the following proteins:
As signature patterns for this class of enzyme, we selected two conserved regions. The first pattern is located in the first half of the sequence and contains two histidine residues that have been shown  to be involved in binding a zinc ion. The second is located in the C-terminal section and contains clustered acidic residues and glycines.Last update:
December 2001 / Pattern and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|Title||The fructose-1,6-bisphosphate aldolases: same reaction, different enzymes.|
|Source||Biochem. Soc. Trans. 18:185-187(1990).|
|2||Authors||Marsh J.J., Lebherz H.G.|
|Title||Fructose-bisphosphate aldolases: an evolutionary history.|
|Source||Trends Biochem. Sci. 17:110-113(1992).|
|3||Authors||von der Osten C.H., Barbas C.F. III, Wong C.-H., Sinskey A.J.|
|Source||Mol. Microbiol. 3:1625-1637(1989).|
|4||Authors||Berry A., Marshall K.E.|
|Title||Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli.|
|Source||FEBS Lett. 318:11-16(1993).|