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Literature summary extracted from

  • Frere, F.; Nentwich, M.; Gacond, S.; Heinz, D.W.; Neier, R.; Frankenberg-Dinkel, N.
    Probing the active site of Pseudomonas aeruginosa porphobilinogen synthase using newly developed inhibitors (2006), Biochemistry, 45, 8243-8253.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.24 hanging drop vapor-diffusion method. Crystal structures of the active site of Pseudomonas aeruginosa PBGS with the various inhibitors 5-hydroxylevulinic acid, 5,5'-oxybis(4-oxopentanoic acid), 5,5'-iminobis(4-oxopentanoic acid), 5,5'-thiobis(4-oxopentanoic acid), 5,5'-sulfinylbis(4-oxopentanoic acid) or 5,5'-sulfonylbis(4-oxopentanoic acid) Pseudomonas aeruginosa

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.24 5,5'-iminobis(4-oxopentanoic acid)
-
 Pseudomonas aeruginosa
4.2.1.24 5,5'-oxybis(4-oxopentanoic acid)
-
 Pseudomonas aeruginosa
4.2.1.24 5,5'-sulfinylbis(4-oxopentanoic acid)
-
 Pseudomonas aeruginosa
4.2.1.24 5,5'-sulfonylbis(4-oxopentanoic acid)
-
 Pseudomonas aeruginosa
4.2.1.24 5,5'-thiobis(4-oxopentanoic acid)
-
 Pseudomonas aeruginosa
4.2.1.24 5-hydroxylevulinic acid
-
 Pseudomonas aeruginosa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.24 Mg2+ enzyme contains Mg2+ in the active site Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.24 5-aminolevulinate + 5-aminolevulinate Pseudomonas aeruginosa porphobilinogen synthase catalyzes the first committed step of the tetrapyrrole biosynthesis pathway porphobilinogen + 2 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.24 Pseudomonas aeruginosa Q59643
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.24
-
 Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.24 5-aminolevulinate + 5-aminolevulinate porphobilinogen synthase catalyzes the first committed step of the tetrapyrrole biosynthesis pathway Pseudomonas aeruginosa porphobilinogen + 2 H2O
-
 ?
4.2.1.24 5-aminolevulinate + 5-aminolevulinate enzymatic mechanism starts with formation of a C-C bond, linking C3 of the A-side 5-aminolevulinic acid to C4 of the P-side 5-aminolevulinic acid through an aldole addition Pseudomonas aeruginosa porphobilinogen + 2 H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.24 PaPBGS
-
 Pseudomonas aeruginosa

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.2.1.24 0.313
-
 5,5'-iminobis(4-oxopentanoic acid) 37°C, pH 8.5 Pseudomonas aeruginosa
4.2.1.24 0.342
-
 5,5'-sulfonylbis(4-oxopentanoic acid) 37°C, pH 8.5 Pseudomonas aeruginosa
4.2.1.24 0.963
-
 5,5'-oxybis(4-oxopentanoic acid) 37°C, pH 8.5 Pseudomonas aeruginosa
4.2.1.24 4.05
-
 5-hydroxylevulinic acid 37°C, pH 8.5 Pseudomonas aeruginosa
4.2.1.24 9.94
-
 5,5'-sulfinylbis(4-oxopentanoic acid) 37°C, pH 8.5 Pseudomonas aeruginosa
4.2.1.24 38.4
-
 5,5'-thiobis(4-oxopentanoic acid) 37°C, pH 8.5 Pseudomonas aeruginosa