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Literature summary for 6.3.3.3 extracted from
- Substrate binding and carboxylation by dethiobiotin synthetase - a kinetic and X-ray study (1995), Curr. Biol., 3, 1207-1215.
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 | ? | - |
? | |
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