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Literature summary for 4.1.2.13 extracted from

  • Baldwin, S.A.; Perham, R.N.
    Novel kinetic and structural properties of the class-I D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain) (1978), Biochem. J., 169, 643-652.
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
2-oxoglutarate enhances D-fructose 1,6-bisphosphate-cleavage activity, fructose 1-phosphate-cleavage activity is unaffected Escherichia coli
citrate enhances activity Escherichia coli
phosphoenolpyruvate enhances D-fructose 1,6-bisphosphate-cleavage activity, fructose 1-phosphate-cleavage activity is unaffected Escherichia coli
sn-glycerol 3-phosphate enhances D-fructose 1,6-bisphosphate-cleavage activity, fructose 1-phosphate-cleavage activity is unaffected Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
140000
-
 gel filtration Escherichia coli
340000
-
 ultracentrifugal analysis Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 Crookes' strain
-
Escherichia coli Crookes
-
 Crookes' strain
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate
-
 Escherichia coli glycerone phosphate + D-glyceraldehyde 3-phosphate
-
 ?
D-fructose 1,6-bisphosphate
-
 Escherichia coli Crookes glycerone phosphate + D-glyceraldehyde 3-phosphate
-
 ?