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Literature summary extracted from
- Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens (2005), FEBS J., 272, 6067-6076.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.2.38 | thiamine diphosphate | the cofactor is fixed at the two ends in separate domains, suspending a comparatively mobile thiazolium ring between them | Pseudomonas fluorescens |  |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.1.2.38 | hanging drop vapour diffusion method, structure of the recombinant seleno-L-methionine-labelled enzyme with bound cofactor thiamine diphosphate at 2.6 A resolution | Pseudomonas fluorescens |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.2.38 | Pseudomonas fluorescens | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.1.2.38 | - |
Pseudomonas fluorescens |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.2.38 | thiamine diphosphate | - |
Pseudomonas fluorescens | |
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