DuraPETase
290 aa · engineered from IsPETase · Cui et al. 2021, ACS Catal.
10 mutations; +31 °C thermostability, ~300x activity
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 · 10 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 | 37.0 °C |
| As published | Published as 37 °C. |
| Optimum pH | not recorded |
| Family | petase_like |
Structure
| Source | ESMFold prediction |
| Mean pLDDT | 96.2 |
| Residues | 290 |
| Cα RMSD to IsPETase | 0.58 Å |
Active site
| Catalytic triad | Ser160 · His237 · Asp206 |
| Ser OG → His NE2 | 2.97 Å |
| His ND1 → Asp OD | 2.71 Å |
| Oxyanion donor 1 | 161 (2.86 Å) |
| Oxyanion donor 2 | 87 (4.48 Å) |
| Cleft width | 23.95 Å |
| Cleft depth | 4.26 Å |
| Cleft residues | 82 |
Aromatic clamp: PHE117 · PHE201 · TRP185 · TYR119 · TYR87
Mutations
S214H, I168R, W159H, S188Q, R280A, A180I, G165A, Q119Y, L117F, T140D
10 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.
Ten-mutation redesign of IsPETase by the GRAPE strategy, Topt 37 C. All ten stated parent residues match IsPETase at offset 0, and the count agrees with the published ten. Ten independent positions agreeing by chance is ~20^-10, so the set is confirmed without needing the supplementary.
Reference: Cui et al. 2021, ACS Catal. doi:10.1021/acscatal.0c05126
Measured activity
| Parameter | Value | Substrate | Evidence | Source |
|---|---|---|---|---|
| performance claim | — | PET | from review | 10.1021/acscatal.0c05126 |
| 10 mutations; +31 °C thermostability, ~300x activity | ||||
| topt | 37.0 degC | PET | from review | 10.1021/acscatal.0c05126 |
| Published as 37 °C. | ||||
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
Ten-mutation redesign of IsPETase by the GRAPE strategy, Topt 37 C. All ten stated parent residues match IsPETase at offset 0, and the count agrees with the published ten. Ten independent positions agreeing by chance is ~20^-10, so the set is confirmed without needing the supplementary.