Literature summary for 4.2.1.24 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	Q59643	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Pseudomonas aeruginosa

Substrates and Products (Substrate)

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

Synonyms	Comment	Organism
PaPBGS	-	Pseudomonas aeruginosa

Ki Value [mM]

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

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Release 2023.1 (January 2023)