Literature summary for 4.2.1.24 extracted from

Frere, F.; Schubert, W.D.; Stauffer, F.; Frankenberg, N.; Neier, R.; Jahn, D.; Heinz, D.W.
Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism (2002), J. Mol. Biol., 320, 237-247.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of the active-site variant D139N of the Mg2+-dependent enzyme in complex with the inhibitor 5-fluorolevulinic acid	Pseudomonas aeruginosa

Inhibitors

Inhibitors	Comment	Organism	Structure
5-fluorolevulinic acid	both inhibitor molecules are covalently bound to two conserved, active-site lysine residues, Lys205 and lys260, through Schiff bases	Pseudomonas aeruginosa

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	dependent on	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	Q59643	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
2 5-aminolevulinate = porphobilinogen + 2 H2O	catalytic mechanism initiated by a C-C bond formation between A and P-side 5-aminolevulinic acid, followed by the formation of the intersubstrate Schiff base yielding the product porphobilinogen	Pseudomonas aeruginosa	a

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Release 2023.1 (January 2023)