{PDOC00143}
{PS00158; ALDOLASE_CLASS_I}
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* Fructose-bisphosphate aldolase class-I active site *
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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.

-Consensus pattern: [LIVM]-x-[LIVMFYW]-E-G-x-[LSI]-L-K-[PA]-[SN]
                    [K is involved in Schiff-base formation]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for Staphylococcus carnosus aldolase.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2006 / Pattern revised.

[ 1] Perham R.N.
     "The fructose-1,6-bisphosphate aldolases: same reaction, different
     enzymes."
     Biochem. Soc. Trans. 18:185-187(1990).
     PubMed=2199259
[ 2] Marsh J.J., Lebherz H.G.
     "Fructose-bisphosphate aldolases: an evolutionary history."
     Trends Biochem. Sci. 17:110-113(1992).
     PubMed=1412694
[ 3] Freemont P.S., Dunbar B., Fothergill-Gilmore L.A.
     "The complete amino acid sequence of human skeletal-muscle
     fructose-bisphosphate aldolase."
     Biochem. J. 249:779-788(1988).
     PubMed=3355497

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