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Literature summary for 4.2.1.24 extracted from

  • Jaffe, E.K.; Kervinen, J.; Martins, J.; Stauffer, F.; Neier, R.; Wlodawer, A.; Zdanov, A.
    Species-specific inhibition of porphobilinogen synthase by 4-oxosebacic acid (2002), J. Biol. Chem., 277, 19792-19799.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of enzyme complexed with 4-oxosebaic acid and of enzyme complexed with 4,7-dioxosebaic acid Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
4,7-dioxosebaic acid
-
Escherichia coli
4-oxosebaic acid active site-directed irreversible inhibitor, less potent than 4,7-dioxosebaic acid Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ enzyme uses a catalytic Zn2+ Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5-aminolevulinate + 5-aminolevulinate Escherichia coli essential step in tetrapyrrole biosynthesis porphobilinogen + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ACB2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-aminolevulinate + 5-aminolevulinate essential step in tetrapyrrole biosynthesis Escherichia coli porphobilinogen + 2 H2O
-
?