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Literature summary extracted from

  • Bevan, D.R.; Bodlaender, P.; Shemin, D.
    Mechanism of porphobilinogen synthase. Requirement of Zn2+ for enzyme activity (1980), J. Biol. Chem., 255, 2030-2035.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.24 1,10-phenanthroline
-
Bos taurus
4.2.1.24 8-Hydroxyquinoline-5-sulfonic acid
-
Bos taurus
4.2.1.24 bathocuproine disulfonic acid
-
Bos taurus
4.2.1.24 EDTA
-
Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.24 Cd2+ can restore activity of the apoenzyme Bos taurus
4.2.1.24 Zn2+ Zn2+ forms a bond with a sulfhydryl group in the enzyme, the octameric enzyme contains 4 gatom of Zn2+ per mol of enzyme, Zn2+ does not participate in substrate binding nor in the maintenance of the quarternary structure of the enzyme Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.24 Bos taurus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.2.1.24 liver
-
Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.24 5-aminolevulinate + 5-aminolevulinate
-
Bos taurus porphobilinogen + 2 H2O
-
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