Z1-PETase
290 aa · engineered from IsPETase · J. Hazard. Mater. 2023
13 mutations, two engineered disulfides; 20x soluble expression yield
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 · 13 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 | 30.0 °C |
| As published | Published as 30 °C. |
| Optimum pH | not recorded |
| Family | petase_like |
Structure
| Source | Experimental, PDB 8H5K |
| Resolution | 1.2 Å |
| Residues | 260 |
| Cα RMSD to IsPETase | 0.39 Å |
Active site
| Catalytic triad | Ser160 · His237 · Asp206 |
| Ser OG → His NE2 | 3.88 Å |
| His ND1 → Asp OD | 3.08 Å |
| Oxyanion donor 1 | 161 (2.57 Å) |
| Oxyanion donor 2 | 87 (3.09 Å) |
| Cleft width | 19.65 Å |
| Cleft depth | 4.12 Å |
| Cleft residues | 81 |
Aromatic clamp: PHE201 · TRP159 · TRP185 · TYR87
Mutations
N37D, S121E, R132E, A171C, A180V, P181V, D186H, S193C, R224E, N233C, S242T, N246D, S282C
13 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.
Thirteen mutations on IsPETase, including two engineered disulfides (A171C-S193C, N233C-S282C) and four shared with FAST-PETase (S121E/D186H/S242T/N246D). Topt 30 C. Confirmed TWICE and independently: the set applies cleanly to IsPETase at offset 0, and all 13 sites read the mutant residue in the deposited 8H5K structure, whose sequence differs from the derived one only by an SHM expression-tag scar and the signal peptide (zero mismatches in the mature region).
Reference: J. Hazard. Mater. 2023 doi:10.1016/j.jhazmat.2023.132297
Measured activity
| Parameter | Value | Substrate | Evidence | Source |
|---|---|---|---|---|
| performance claim | — | PET | from review | 10.1016/j.jhazmat.2023.132297 |
| 13 mutations, two engineered disulfides; 20x soluble expression yield | ||||
| topt | 30.0 degC | PET | from review | 10.1016/j.jhazmat.2023.132297 |
| Published as 30 °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
Thirteen mutations on IsPETase, including two engineered disulfides (A171C-S193C, N233C-S282C) and four shared with FAST-PETase (S121E/D186H/S242T/N246D). Topt 30 C. Confirmed TWICE and independently: the set applies cleanly to IsPETase at offset 0, and all 13 sites read the mutant residue in the deposited 8H5K structure, whose sequence differs from the derived one only by an SHM expression-tag scar and the signal peptide (zero mismatches in the mature region).