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Literature summary extracted from

  • Schwartz, N.B.; Abram, D.; Feingold, D.S.
    L-Rhamnulose 1-phosphate aldolase of Escherichia coli. The role of metal in enzyme structure (1974), Biochemistry, 13, 1726-1730.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.2.19 5,5'-dithiobis(2-nitrobenzoate)
-
Escherichia coli
4.1.2.19 p-mercuribenzoate
-
Escherichia coli
4.1.2.19 SDS competitive with L-rhamnulose 1-phosphate or glycerone phosphate, noncompetitive with L-lactaldehyde 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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.2.19 35000
-
4 * 35000 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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Subunits

EC Number Subunits Comment Organism
4.1.2.19 tetramer 4 * 35000 Escherichia coli