Literature summary for 4.2.1.24 extracted from

Frankenberg, N.; Jahn, D.; Jaffe, E.K.
Pseudomonas aeruginosa contains a novel type V porphobilinogen synthase with no required catalytic metal ions (1999), Biochemistry, 38, 13976-13982.

Search for more literature for 4.2.1.24

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	binds only 4 Mg2+ per octamer, these 4 Mg2+ allosterically stimulate a metal ion independent catalytic actiovity, in a fashion dependent upon both pH and K+, the allosteric Mg2+ is located in metal binding site C, which is outside the active site. NO evidence is found for metal binding to the potential high-affinity active site metal binding site A and/or B, no direct involvement of Mg2+ in substrate binding and product formation	Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
5-aminolevulinate	Pseudomonas aeruginosa	enzyme catalyzes the first common step in tetrapyrrole biosynthesis	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5-aminolevulinate	enzyme catalyzes the first common step in tetrapyrrole biosynthesis	Pseudomonas aeruginosa	?	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)