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PROSITE documentation PDOC00143

Fructose-bisphosphate aldolase class-I active site





Description

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.

Technical section

PROSITE method (with tools and information) covered by this documentation:

ALDOLASE_CLASS_I, PS00158; Fructose-bisphosphate aldolase class-I active site  (PATTERN)


References

1AuthorsPerham R.N.
TitleThe fructose-1,6-bisphosphate aldolases: same reaction, different enzymes.
SourceBiochem. Soc. Trans. 18:185-187(1990).
PubMed ID2199259

2AuthorsMarsh J.J., Lebherz H.G.
TitleFructose-bisphosphate aldolases: an evolutionary history.
SourceTrends Biochem. Sci. 17:110-113(1992).
PubMed ID1412694

3AuthorsFreemont P.S., Dunbar B., Fothergill-Gilmore L.A.
TitleThe complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase.
SourceBiochem. J. 249:779-788(1988).
PubMed ID3355497



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