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Literature summary extracted from

  • Kochman, M.; Hargrave, P.A.; Buczylko, J.
    Fructose-bisphosphate aldolase from Helix pomatia (1982), Methods Enzymol., 90, 259-263.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.2.13 ADP
-
Helix pomatia
4.1.2.13 AMP
-
Helix pomatia
4.1.2.13 ATP
-
Helix pomatia
4.1.2.13 NaBH4 in presence of substrate Helix pomatia

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.2.13 0.0003
-
D-fructose 1,6-bisphosphate
-
Helix pomatia
4.1.2.13 1
-
fructose 1-phosphate
-
Helix pomatia

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.13 Helix pomatia
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.2.13
-
Helix pomatia

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.13 D-fructose 1,6-bisphosphate
-
Helix pomatia glycerone phosphate + D-glyceraldehyde 3-phosphate
-
?
4.1.2.13 D-Fructose 1-phosphate 5% of the activity with fructose 1,6-diphosphate Helix pomatia Glycerone phosphate + D-glyceraldehyde
-
?