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