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Literature summary for 2.2.1.5 extracted from
- A protecting group-free synthesis of deazathiamine: a step toward inhibitor design (2010), Bioorg. Med. Chem. Lett., 20, 6472-6474.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| deazathiamine | - |
Mycobacterium tuberculosis |  |
| deazathiamine diphosphate | binds 32fold more tightly to the enzyme than thiamine diphosphate | Mycobacterium tuberculosis | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | - |
- |
- |
IC50 Value
| IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|
| 0.0067 | - |
pH not specified in the publication, temperature not specified in the publication | Mycobacterium tuberculosis | deazathiamine diphosphate | |
| 0.144 | - |
pH not specified in the publication, temperature not specified in the publication | Mycobacterium tuberculosis | deazathiamine | |
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Release 2023.1 (January 2023)
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