DepoPETase
290 aa · engineered from IsPETase · Shi et al. 2023, Angew. Chem. Int. Ed.
7 mutations; melting temperature +23.3 °C, ~1407x product
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 · 7 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 | Published as ~50 °C (applied). |
| Optimum pH | not recorded |
| Family | petase_like |
Structure
| Source | ESMFold prediction |
| Mean pLDDT | 96.3 |
| Residues | 290 |
| Cα RMSD to IsPETase | 0.59 Å |
Active site
| Catalytic triad | Ser160 · His237 · Asp206 |
| Ser OG → His NE2 | 2.97 Å |
| His ND1 → Asp OD | 2.79 Å |
| Oxyanion donor 1 | 161 (2.86 Å) |
| Oxyanion donor 2 | 87 (4.52 Å) |
| Cleft width | 19.46 Å |
| Cleft depth | 4.27 Å |
| Cleft residues | 83 |
Aromatic clamp: PHE201 · TRP159 · TRP185 · TYR87
Mutations
T88I, D186H, D220N, N233K, N246D, R260Y, S290P
7 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.
Seven-mutation IsPETase from flexible-loop directed evolution: Tm +23.3 C and ~1407-fold more product than wild type. All seven match at offset 0.
Reference: Shi et al. 2023, Angew. Chem. Int. Ed. doi:10.1002/anie.202218390
Measured activity
| Parameter | Value | Substrate | Evidence | Source |
|---|---|---|---|---|
| performance claim | — | PET | from review | 10.1002/anie.202218390 |
| 7 mutations; melting temperature +23.3 °C, ~1407x product | ||||
| topt | 50.0 degC | PET | from review | 10.1002/anie.202218390 |
| Published as ~50 °C (applied). | ||||
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
Seven-mutation IsPETase from flexible-loop directed evolution: Tm +23.3 C and ~1407-fold more product than wild type. All seven match at offset 0.