LCC
Unknown prokaryotic organism · 293 aa · UniProt
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
catalytic triad · the same colours as the viewer above. Triad positions are labelled; hover any residue for its number. Click one to select it in both.
MDGVLWRVRTAALMAALLALAAWALVWASPSVEAQSNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDYPDSRASQLSAALNYLRTSSPSAVRARLDANRLAVAGH165SMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTSVPVLIVGAEA210DTVAPVSQHAIPFYQNLPSTTPKVYVELDNAS242HFAPNSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALSDFRTNNRHCQ
Activity
| Optimum temperature | 70.0 °C |
| As published | On PET the optimum is SUPERIOR TO 70 degrees Celsius (PubMed:22194294); 70 is stored as a lower bound, not a measured optimum. The previously stored 50 degrees is the optimum on pNP-butanoate (PubMed:22194294, PubMed:24593046), a model ester rather than PET. Rule 1: prefer the PET substrate. |
| Optimum pH | 8.5 |
| Family | cutinase |
Structure
| Source | Experimental, PDB 4EB0 |
| Resolution | 1.5 Å |
| Residues | 258 |
| Cα RMSD to IsPETase | 1.54 Å |
Active site
| Catalytic triad | Ser165 · His242 · Asp210 |
| Ser OG → His NE2 | 2.45 Å |
| His ND1 → Asp OD | 2.75 Å |
| Oxyanion donor 1 | 166 (3.26 Å) |
| Oxyanion donor 2 | 95 (5.32 Å) |
| Cleft width | 24.22 Å |
| Cleft depth | 4.35 Å |
| Cleft residues | 85 |
Aromatic clamp: PHE125 · PHE222 · PHE243 · TRP190 · TYR127 · TYR223 · TYR95
Measured activity
| Parameter | Value | Substrate | Evidence | Source |
|---|---|---|---|---|
| catalytic activity | — | PET | measured | PMID 22194294 · PMID 32269349 |
| (ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+) | ||||
| km | 0.21 mM | pNP-butanoate (at 50 degrees Celsius and pH 8.0) | measured | PMID 24593046 |
| km | 0.22 mM | pNP-butanoate (at 30 degrees Celsius and pH 8.0) | measured | PMID 24593046 |
| km | 0.24 mM | pNP-butanoate (at 70 degrees Celsius and pH 8.0) | measured | PMID 24593046 |
| ph opt | 8.5 pH | — | measured | PMID 22194294 |
| Optimum pH is 8.5 with pNP-butyrate as substrate. Shows 70% of the maximal activity at pH 7.0 and pH 9.5. | ||||
| topt | 70.0 degC | — | measured | PMID 22194294 · PMID 24593046 · PMID 32269349 |
| On PET the optimum is SUPERIOR TO 70 degrees Celsius (PubMed:22194294); 70 is stored as a lower bound, not a measured optimum. The previously stored 50 degrees is the optimum on pNP-butanoate (PubMed:22194294, PubMed:24593046), a model ester rather than PET. Rule 1: prefer the PET substrate. | ||||
Related in PANTS
Identifiers and cross-references
Structure
Sequence
Leaf-branch compost cutinase, metagenome-derived. Parent of the LCC-ICCG industrial variant. 293 aa.