| Fructose-bisphosphate aldolase class-I | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| fructose 1,6-bisphosphate aldolase from rabbit liver | |||||||||
| Identifiers | |||||||||
| Symbol | Glycolytic | ||||||||
| Pfam | PF00274 | ||||||||
| InterPro | IPR000741 | ||||||||
| PROSITE | PDOC00143 | ||||||||
| SCOP | 1ald | ||||||||
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| Fructose-bisphosphate aldolase class-II | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| class ii fructose-1,6-bisphosphate aldolase in complex with phosphoglycolohydroxamate | |||||||||
| Identifiers | |||||||||
| Symbol | F_bP_aldolase | ||||||||
| Pfam | PF01116 | ||||||||
| Pfam clan | CL0036 | ||||||||
| InterPro | IPR000771 | ||||||||
| PROSITE | PDOC00523 | ||||||||
| SCOP | 1dos | ||||||||
|
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In molecular biology, fructose-bisphosphate aldolase EC 4.1.2.13,[1][2] 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[3] are found in animals, 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 are produced in bacteria and fungi, and require an active-site divalent metal ion.[2]
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 B result in hereditary fructose intolerance.
Class II aldolases,[2] mainly found in prokaryotes and fungi, are homodimeric enzymes, which require a divalent metal ion, generally zinc, for their activity. The class II aldolase family of proteins also includes subfamilies containing the Escherichia coli galactitol operon protein, gatY, which catalyses the transformation of tagatose 1,6-bisphosphate into glycerone phosphate and D-glyceraldehyde 3-phosphate (EC 4.1.2.40); and E. coli N-acetyl galactosamine operon protein, agaY, which catalyses the same reaction. There are two histidine residues in the first half of the sequence of these enzymes that have been shown to be involved in binding a zinc ion.[4]
This article incorporates text from the public domain Pfam and InterPro IPR000741
This article incorporates text from the public domain Pfam and InterPro IPR000771