FAST-PETase
290 aa · engineered from IsPETase · Lu et al. 2022, Nature (MutCompute)
38x activity over ThermoPETase, its scaffold; 33.8 mM monomers in 96 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 290 aa · 5 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. 38x activity over IsPETase; 33.8 mM monomers in 96 h. Primary reference: Lu et al. 2022, Nature. 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 | Experimental, PDB 7SH6 |
| Resolution | 1.44 Å |
| Residues | 261 |
| Cα RMSD to IsPETase | 0.13 Å |
Active site
| Catalytic triad | Ser160 · His237 · Asp206 |
| Ser OG → His NE2 | 2.85 Å |
| His ND1 → Asp OD | 3.01 Å |
| Oxyanion donor 1 | 161 (3.32 Å) |
| Oxyanion donor 2 | 87 (5.61 Å) |
| Cleft width | 22.16 Å |
| Cleft depth | 4.32 Å |
| Cleft residues | 84 |
Aromatic clamp: PHE201 · TRP159 · TRP185 · TYR219 · TYR87
Mutations
S121E, D186H, R224Q, N233K, R280A
5 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.
ThermoPETase scaffold plus R224Q/N233K. Machine-learning designed. HAS an experimental structure, contrary to a first look: 7SH6 appears to carry 19 substitutions against IsPETase, but 14 of those are a heterologous secretion leader replacing the native signal peptide, and its MATURE chain (residue 28 on) is identical to FAST-PETase. 8J45 is the same protein again, expressed in Pichia pastoris, differing only by an EF cloning scar where the mature sequence begins QT. Comparing whole precursors instead of mature chains is what hid this.
Reference: Lu et al. 2022, Nature (MutCompute) doi:10.1038/s41586-022-04599-z
Measured activity
| Parameter | Value | Substrate | Evidence | Source |
|---|---|---|---|---|
| performance claim | — | PET | from review | 10.1038/s41586-022-04599-z |
| 38x activity over ThermoPETase, its scaffold; 33.8 mM monomers in 96 h | ||||
| topt | 50.0 degC | PET | from review | 10.1038/s41586-022-04599-z |
| Optimum temperature 50 degC. 38x activity over IsPETase; 33.8 mM monomers in 96 h. Primary reference: Lu et al. 2022, Nature. 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
ThermoPETase scaffold plus R224Q/N233K. Machine-learning designed. HAS an experimental structure, contrary to a first look: 7SH6 appears to carry 19 substitutions against IsPETase, but 14 of those are a heterologous secretion leader replacing the native signal peptide, and its MATURE chain (residue 28 on) is identical to FAST-PETase. 8J45 is the same protein again, expressed in Pichia pastoris, differing only by an EF cloning scar where the mature sequence begins QT. Comparing whole precursors instead of mature chains is what hid this.