BRENDA - Enzyme Database show

Pseudomonas aeruginosa contains a novel type V porphobilinogen synthase with no required catalytic metal ions

Frankenberg, N.; Jahn, D.; Jaffe, E.K.; Biochemistry 38, 13976-13982 (1999)

Data extracted from this reference:

Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
4.2.1.24
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)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.2.1.24
5-aminolevulinate
Pseudomonas aeruginosa
enzyme catalyzes the first common step in tetrapyrrole biosynthesis
?
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.24
Pseudomonas aeruginosa
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.24
5-aminolevulinate
enzyme catalyzes the first common step in tetrapyrrole biosynthesis
210731
Pseudomonas aeruginosa
?
-
-
-
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
4.2.1.24
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) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.2.1.24
5-aminolevulinate
Pseudomonas aeruginosa
enzyme catalyzes the first common step in tetrapyrrole biosynthesis
?
-
-
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.24
5-aminolevulinate
enzyme catalyzes the first common step in tetrapyrrole biosynthesis
210731
Pseudomonas aeruginosa
?
-
-
-
-