PROSITE documentation PDOC00143Fructose-bisphosphate aldolase class-I active site
Fructose-bisphosphate aldolase (EC 4.1.2.13) [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 [3], 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.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Perham R.N. |
| Title | The fructose-1,6-bisphosphate aldolases: same reaction, different enzymes. | |
| Source | Biochem. Soc. Trans. 18:185-187(1990). | |
| PubMed ID | 2199259 |
| 2 | Authors | Marsh J.J. Lebherz H.G. |
| Title | Fructose-bisphosphate aldolases: an evolutionary history. | |
| Source | Trends Biochem. Sci. 17:110-113(1992). | |
| PubMed ID | 1412694 |
| 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). | |
| PubMed ID | 3355497 |
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