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Literature summary extracted from

  • Kundrat, L.; Martins, J.; Stith, L.; Dunbrack, R.L., Jr.; Jaffe, E.K.
    A structural basis for half-of-the-sites metal binding revealed in Drosophila melanogaster porphobilinogen synthase (2003), J. Biol. Chem., 278, 31325-31330.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.24
-
 Drosophila melanogaster

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.24 H10F mutant enzyme is active but is not inhibited by zinc. H10F binds a catalytic zinc at 0.5/subunit and binds a second nonessential and noninhibitory zinc at 0.5/subunit Drosophila melanogaster

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.24 Zn2+ the inhibitory zinc is located at a subunit interface using Cys219 and His10 as ligands Drosophila melanogaster

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.24 0.108
-
 5-aminolevulinate pH 8 Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.24 Drosophila melanogaster
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.24
-
 Drosophila melanogaster

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.24 0.283
-
-
 Drosophila melanogaster

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.24 5-aminolevulinate + 5-aminolevulinate
-
 Drosophila melanogaster porphobilinogen + 2 H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.24 PBGS
-
 Drosophila melanogaster