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Literature summary extracted from

  • Schwartz, N.B.; Feingold, D.S.
    L-Rhamnulose 1-phosphate aldolase from Escherichia coli. III. The role of divalent cations in enzyme activity (1972), Bioorg. Chem., 2, 75-86.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.2.19 1,10-phenanthroline competitive with L-rhamnulose 1-phosphate or glycerone phosphate Escherichia coli
4.1.2.19 8-hydroxyquinoline 5-sulfonic acid
-
Escherichia coli
4.1.2.19 p-mercuribenzoate
-
Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.2.19 Zn zinc metalloenzyme Escherichia coli
4.1.2.19 Zn contains 2 gatom of zinc per mol of enzyme Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.19 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.19 L-Rhamnulose 1-phosphate
-
Escherichia coli Glycerone phosphate + (S)-lactaldehyde
-
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