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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.

April 2006 / Pattern revised.

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

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

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

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00158 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00158 • Scan Swiss-Prot/TrEMBL entries against PS00158 • view ligand binding statistics

Matching PDB structures: 1A5C 1ADO 1ALD 1EWD ... [ALL]

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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