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Literature summary for 3.1.1.101 extracted from
- Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca (2014), Appl. Microbiol. Biotechnol., 98, 7815-7823.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Thermobifida fusca |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| molecular replacement with a poly-Ala model of Streptomyces exofoliatus lipase, PDB-ID: 1JFR, in free as well as in inhibitor-bound form. The enzyme forms a classical alpha/beta-hydrolase fold with a central nine-stranded beta-sheet flanked by 11 alpha-helices on both sides. The catalytic triad, comprising S130, D176 and H208, is located in a crevice on the surface of the enzyme | Thermobifida fusca |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| PMSF | the PMSF protein complex reveals covalent modification of S130 and binding of one of the oxygens of the tetrahedral adduct in the oxyanion hole formed by the main chain nitrogens of M131 and Y60 | Thermobifida fusca |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermobifida fusca | E5BBQ3 | cf. EC 3.1.1.74 | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cut-2.KW3 | - |
Thermobifida fusca |
| cutinase | - |
Thermobifida fusca |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 61 | - |
loss of activity above | Thermobifida fusca |
| 70 | - |
melting temperature | Thermobifida fusca |
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Release 2023.1 (January 2023)
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