Conserved Site

Fructose-bisphosphate aldolase class-I active site (IPR029768)

Short name: Aldolase_I_AS

Description

Fructose-bisphosphate aldolase (EC:4.1.2.13) [PMID: 2199259, PMID: 1412694] is a glycolytic enzyme that catalyses 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 enzymes [PMID: 3355497] do not require a metal ion, and are characterised by the formation of a Schiff base intermediate between a highly conserved active site lysine and a substrate carbonyl group, while the class II enzymes require an active-site divalent metal ion. This entry represents the class I enzymes.

In vertebrates, three forms of this enzyme are found: aldolase A is expressed in muscle, aldolase B in liver, kidney, stomach and intestine, and aldolase C in brain, heart and ovary. The different isozymes have different catalytic functions: aldolases A and C are mainly involved in glycolysis, while aldolase B is involved in both glycolysis and gluconeogenesis. Defects in aldolase A cause Glycogen storage disease 12 (GSD12) [PMID: 14766013], while defects in aldolase B result in hereditary fructose intolerance [PMID: 15880727].

This conserved site represents the sequence around the lysine involved in the Schiff-base.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns