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Literature summary extracted from
- Computational insights into the mechanism of porphobilinogen synthase (2010), J. Phys. Chem. B, 114, 16860-16870.
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.24 | Zn2+ | required for catalysis, bound at the active site | Saccharomyces cerevisiae |  |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.24 | 2 5-aminolevulinate | Saccharomyces cerevisiae | - |
porphobilinogen + 2 H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.24 | Saccharomyces cerevisiae | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 4.2.1.24 | 2 5-aminolevulinate = porphobilinogen + 2 H2O | reaction mechanism involving asymmetric addition and cyclization of two 5-aminolevulinate molecules, modeling, detailed overview. The active site consists of several invariant residues, including two lysyl residues Lys210 and Lys263 that bind the two substrate moieties as Schiff bases, active site structure and substrate binding, overview. The intersubstrate C-N bond is formed first have a rate-limiting barrier that is lower than those in which the intersubstrate C-C bond is formed first | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.24 | 2 5-aminolevulinate | - |
Saccharomyces cerevisiae | porphobilinogen + 2 H2O | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.1.24 | PBGS | - |
Saccharomyces cerevisiae |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.2.1.24 | metabolism | PBGS is a key enzyme in heme biosynthesis | Saccharomyces cerevisiae |
| 4.2.1.24 | physiological function | PBGS is a key enzyme in heme biosynthesis that catalyzes the formation of porphobilinogen from two 5-aminolevulinic acid molecules via formation of intersubstrate C-N and C-C bonds | Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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