TurboPETase
293 aa · engineered from BhrPETase · Cui et al. 2024, Nat. Commun. 15:1417
98.2% depolymerisation at 200 g/kg in 8 h
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 293 aa · 8 substitutions
catalytic triad substitution against BhrPETase · 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 | 65.0 °C |
| As published | The primary paper (doi:10.1038/s41467-024-45662-9) runs its depolymerisation at 65 degrees Celsius and never reports an optimum for TurboPETase: it tests 50, 60 and 65 and 65 performs best of those three. The previously stored '65 to 68' interval does not appear in it, and may have been conflated with the melting temperature of 84 degrees. Stored as the operating temperature, not a measured optimum. |
| Optimum pH | not recorded |
| Family | petase_like |
Structure
| Source | ESMFold prediction |
| Mean pLDDT | 94.2 |
| Residues | 293 |
| Cα RMSD to IsPETase | 1.64 Å |
Active site
| Catalytic triad | Ser165 · His242 · Asp210 |
| Ser OG → His NE2 | 2.99 Å |
| His ND1 → Asp OD | 2.98 Å |
| Oxyanion donor 1 | 166 (2.88 Å) |
| Oxyanion donor 2 | 95 (4.50 Å) |
| Cleft width | 8.70 Å |
| Cleft depth | 4.37 Å |
| Cleft residues | 82 |
Aromatic clamp: PHE127 · TRP190 · TYR95
Mutations
H218S, F222I, A209R, D238K, A251C, A281C, W104L, F243T
8 substitutions against BhrPETase. 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.
Eight mutations on BhrPETase, NOT on IsPETase: the parent recorded here before curation was wrong. Grouped by what they do: substrate-binding cleft flexibility (H218S/F222I, W104L, F243T), surface charge-charge optimisation (A209R, D238K) and one engineered disulfide (A251C-A281C). All eight match BhrPETase at offset 0. doi:10.1038/s41467-024-45662-9
Reference: Cui et al. 2024, Nat. Commun. 15:1417 doi:10.1038/s41467-024-45662-9
Measured activity
| Parameter | Value | Substrate | Evidence | Source |
|---|---|---|---|---|
| performance claim | — | PET | from review | 10.1038/s41467-024-45662-9 |
| 98.2% depolymerisation at 200 g/kg in 8 h | ||||
| topt | 65.0 degC | PET | from review | 10.1038/s41467-024-45662-9 |
| The primary paper (doi:10.1038/s41467-024-45662-9) runs its depolymerisation at 65 degrees Celsius and never reports an optimum for TurboPETase: it tests 50, 60 and 65 and 65 performs best of those three. The previously stored '65 to 68' interval does not appear in it, and may have been conflated with the melting temperature of 84 degrees. Stored as the operating temperature, not a measured optimum. | ||||
Related in PANTS
Lineage
Engineered from BhrPETase.
Nearest metagenomic candidates
No candidate in the catalogue names this enzyme as its nearest match.
Identifiers and cross-references
Activity
Internal
Eight mutations on BhrPETase, NOT on IsPETase: the parent recorded here before curation was wrong. Grouped by what they do: substrate-binding cleft flexibility (H218S/F222I, W104L, F243T), surface charge-charge optimisation (A209R, D238K) and one engineered disulfide (A251C-A281C). All eight match BhrPETase at offset 0. doi:10.1038/s41467-024-45662-9