|PROSITE documentation PDOC00143|
Fructose-bisphosphate aldolase (EC 184.108.40.206) [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-I aldolases , mainly found in higher eukaryotes, are homotetrameric enzymes which form a Schiff-base intermediate between the C-2 carbonyl group of the substrate (dihydroxyacetone phosphate) and the epsilon-amino group of a lysine residue.
In vertebrates, three forms of this enzyme are found: aldolase A in muscle, aldolase B in liver and aldolase C in brain.
The sequence around the lysine involved in the Schiff-base is highly conserved and can be used as a signature for this class of enzyme.Last update:
April 2006 / Pattern revised.
PROSITE method (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||Freemont P.S., Dunbar B., Fothergill-Gilmore L.A.|
|Title||The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase.|
|Source||Biochem. J. 249:779-788(1988).|