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Literature summary extracted from
- High resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis. Implications for substrate activation in pyruvate decarboxylases (1998), J. Biol. Chem., 273, 20196-20204.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.1.1.1 | expression in Escherichia coli | Zymomonas mobilis |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.1.1.1 | - |
Zymomonas mobilis |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.1.1 | Zymomonas mobilis | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.1 | pyruvate | - |
Zymomonas mobilis | acetaldehyde + CO2 | - |
? |  |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.1.1.1 | tetramer | two of the dimers form a tightly packed tetramer with pseudo 222 symmetry | Zymomonas mobilis |
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Release 2023.1 (January 2023)
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