Protein Domain : Fructose-bisphosphate aldolase, class-I IPR000741

Type  Family
Description  Fructose-bisphosphate aldolase ( ) [ , ] 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 [ ] 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) [], while defects in aldolase B result in hereditary fructose intolerance [].
Short Name  FBA_I

1 Child Features

3 Gene Families

821 Genes

2 Ontology Annotations

0 Parent Features

14 Publications

USDA
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