LCC-ICCG
293 aa · engineered from LCC · Tournier et al. 2020, Nature
~90% depolymerisation of pretreated PET in under 10 h at 200 g/kg, 72 °C
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 · 4 substitutions
catalytic triad substitution against LCC · 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 | 68.5 °C |
| As published | Optimum temperature 68.5 degC. reported as 65-72 degC; midpoint recorded. 1.3 g PET waste in 3 days from 1.25 mg enzyme. Primary reference: Tournier et al. 2020, 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 | cutinase |
Structure
| Source | Experimental, PDB 6THT |
| Resolution | 1.14 Å |
| Deposit | catalytically inactivated |
| Residues | 258 |
| Cα RMSD to IsPETase | 1.56 Å |
Active site
No triad measured. Either no structure was built, or the three residues are present in sequence but not connected in space, which is the distinction the geometry stage exists to make.
Mutations
F243I, D238C, S283C, Y127G
4 substitutions against LCC. 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.
STRUCTURE CAVEAT: 6THT is the CATALYTICALLY INACTIVATED form. Its title, 'quintuple variant', is ICCG's four substitutions plus S165A -- the catalytic serine replaced by alanine so the enzyme could be crystallised with substrate bound. Residue 165 in that model is ALA, which is why no triad can be measured from it: the nucleophile is not there. The other deposit from the same paper, 6THS, is the same knockout on wild-type LCC, and 7VVE carries S165A too, so no active LCC-ICCG structure appears to exist. The sequence stored here is derived from the mutation list and is the ACTIVE enzyme; only the coordinates are the inactivated form. Same trap as 7CEH and the PHL7 entry. The industrial benchmark: D238C/S283C disulfide plus F243I/Y127G. Numbering is checked against the parent by apply_mutations; if the literature counts from the mature protein the offset is reported rather than guessed at.
Reference: Tournier et al. 2020, Nature doi:10.1038/s41586-020-2149-4
Measured activity
| Parameter | Value | Substrate | Evidence | Source |
|---|---|---|---|---|
| performance claim | — | PET | from review | 10.1038/s41586-020-2149-4 |
| ~90% depolymerisation of pretreated PET in under 10 h at 200 g/kg, 72 °C | ||||
| topt | 68.5 degC | PET | from review | 10.1038/s41586-020-2149-4 |
| Optimum temperature 68.5 degC. reported as 65-72 degC; midpoint recorded. 1.3 g PET waste in 3 days from 1.25 mg enzyme. Primary reference: Tournier et al. 2020, 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 LCC.
Nearest metagenomic candidates
No candidate in the catalogue names this enzyme as its nearest match.
Identifiers and cross-references
STRUCTURE CAVEAT: 6THT is the CATALYTICALLY INACTIVATED form. Its title, 'quintuple variant', is ICCG's four substitutions plus S165A -- the catalytic serine replaced by alanine so the enzyme could be crystallised with substrate bound. Residue 165 in that model is ALA, which is why no triad can be measured from it: the nucleophile is not there. The other deposit from the same paper, 6THS, is the same knockout on wild-type LCC, and 7VVE carries S165A too, so no active LCC-ICCG structure appears to exist. The sequence stored here is derived from the mutation list and is the ACTIVE enzyme; only the coordinates are the inactivated form. Same trap as 7CEH and the PHL7 entry. The industrial benchmark: D238C/S283C disulfide plus F243I/Y127G. Numbering is checked against the parent by apply_mutations; if the literature counts from the mature protein the offset is reported rather than guessed at.