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Literature summary for 6.3.3.3 extracted from

  • Alexeev, D.; Baxter, R.L.; Smekal, O.; Sawyer, L.
    Substrate binding and carboxylation by dethiobiotin synthetase - a kinetic and X-ray study (1995), Curr. Biol., 3, 1207-1215.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ essential cofactor for both substrate binding and carbamate formation Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 7,8-diaminononanoate + CO2 Escherichia coli penultimate enzyme of biotin biosynthesis ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + 7,8-diaminononanoate + CO2 = ADP + phosphate + dethiobiotin mechanistic model in which binding of Mg2+ and the triphosphate element of ATP to the enzyme creates the appropriate geometry for substrate 7,8-diaminononanoate-binding and carbamate formation Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 7,8-diaminononanoate + CO2
-
Escherichia coli ADP + phosphate + dethiobiotin
-
?
ATP + 7,8-diaminononanoate + CO2 penultimate enzyme of biotin biosynthesis Escherichia coli ?
-
?