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Literature summary extracted from
- Insights into the Substrate Specificity of a Thioesterase Rv0098 of Mycobacterium Tuberculosis through X-ray Crystallographic and Molecular Dynamics Studies (2012), J. Biomol. Struct. Dyn., 29, 973-983.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.1.2.20 | crystal structure of Rv0098 bound to dodecanoic acid is shown | Mycobacterium tuberculosis |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.2.20 | Mycobacterium tuberculosis | P9WM67 | - |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.1.2.20 | an acyl-CoA + H2O = CoA + a carboxylate | molecular dynamics studies show that certain residues of the substrate binding tunnel are flexibel and thus modulate the length of the tunnel | Mycobacterium tuberculosis |
aSynonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.2.20 | Rv0098 | locus name | Mycobacterium tuberculosis |
| 3.1.2.20 | thioesterase | - |
Mycobacterium tuberculosis |
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