ThermoPETase
290 aa · engineered from IsPETase · Son et al. 2019, ACS Catal.
3 mutations; the thermostabilised scaffold FAST-PETase was built on
Structure, superposed on IsPETase
Aligned onto IsPETase 6EQE when it was written, so anything added below overlays directly and the browser does no alignment. The catalytic triad is drawn from the residues the geometry stage measured, not from positions inferred by an alignment.
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Sequence 290 aa · 3 substitutions
catalytic triad substitution against IsPETase · the same colours as the viewer above. Triad positions are labelled; hover any residue for its number. Click one to select it in both.
Activity
| Optimum temperature | 50.0 °C |
| As published | Optimum temperature 50 degC. thermostabilised IsPETase scaffold that FAST-PETase was built on. Primary reference: Son et al. 2019, ACS Catal.. Value taken from a secondary review, NOT from the primary paper and NOT carrying an ECO evidence code: weaker provenance than the UniProt-extracted rows. |
| Optimum pH | not recorded |
| Family | petase_like |
Structure
| Source | ESMFold prediction |
| Mean pLDDT | 96.2 |
| Residues | 290 |
| Cα RMSD to IsPETase | 0.56 Å |
Active site
| Catalytic triad | Ser160 · His237 · Asp206 |
| Ser OG → His NE2 | 2.96 Å |
| His ND1 → Asp OD | 2.79 Å |
| Oxyanion donor 1 | 161 (2.85 Å) |
| Oxyanion donor 2 | 87 (4.52 Å) |
| Cleft width | 19.48 Å |
| Cleft depth | 4.28 Å |
| Cleft residues | 82 |
Aromatic clamp: PHE201 · TRP159 · TRP185 · TYR87
Mutations
S121E, D186H, R280A
3 substitutions against IsPETase. Every one was applied by a routine that refuses any substitution whose stated parent residue does not match, so a wrong position or a mature-versus-precursor numbering shift fails loudly rather than producing a plausible but wrong sequence.
Thermostabilised IsPETase, the scaffold FAST-PETase was built on.
Reference: Son et al. 2019, ACS Catal. doi:10.1021/acscatal.9b00568
Measured activity
| Parameter | Value | Substrate | Evidence | Source |
|---|---|---|---|---|
| performance claim | — | PET | from review | 10.1021/acscatal.9b00568 |
| 3 mutations; the thermostabilised scaffold FAST-PETase was built on | ||||
| topt | 50.0 degC | PET | from review | 10.1021/acscatal.9b00568 |
| Optimum temperature 50 degC. thermostabilised IsPETase scaffold that FAST-PETase was built on. Primary reference: Son et al. 2019, ACS Catal.. Value taken from a secondary review, NOT from the primary paper and NOT carrying an ECO evidence code: weaker provenance than the UniProt-extracted rows. | ||||
Related in PANTS
Lineage
Engineered from IsPETase.
Nearest metagenomic candidates
No candidate in the catalogue names this enzyme as its nearest match.
Identifiers and cross-references
Activity
Internal
Thermostabilised IsPETase, the scaffold FAST-PETase was built on.