Description

IPR029768 is a Fructose-bisphosphate aldolase class-I active site.

<p>Fructose-bisphosphate aldolase ([ec:4.1.2.13]) [[cite:PUB00000567], [cite:PUB00005383]] 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 [[cite:PUB00000463]] 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.</p> <p>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) [[cite:PUB00070914]], while defects in aldolase B result in hereditary fructose intolerance [[cite:PUB00070915]].</p> <p>This conserved site represents the sequence around the lysine involved in the Schiff-base.</p>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 17

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: