########     ###    ##    ## ########  ######  
##     ##   ## ##   ###   ##    ##    ##    ## 
##     ##  ##   ##  ####  ##    ##    ##       
########  ##     ## ## ## ##    ##     ######  
##        ######### ##  ####    ##          ## 
##        ##     ## ##   ###    ##    ##    ## 
##        ##     ## ##    ##    ##     ######  

PETase ANnotation and Triage System

Nature's solution to a human-made health problem

IsPETase

Piscinibacter sakaiensis · 290 aa · UniProt

Wild type; weak on crystalline PET

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.

Overlay another

Sequence 290 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.

MNFPRASRLMQAAVLGGLMAVSAAATAQTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVPGYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPSSRSSQQMAALRQVASLNGTSSSPIYGKVDTARMGVMGW160SMGGGGSLISAANNPSLKAAAPQAPWDSSTNFSSVTVPTLIFACEN206DSIAPVNSSALPIYDSMSRNAKQFLEINGGS237HSCANSGNSNQALIGKKGVAWMKRFMDNDTRYSTFACENPNSTRVSDFRTANCS

Activity

Optimum temperature40.0 °C
As publishedOptimum temperature is 40 degrees Celsius for PET film hydrolysis (PubMed:26965627). Optimum temperature is 30 degrees Celsius for PET (commercial drinking bottle) hydrolysis and BHET hydrolysis (PubMed:29603535). Optimum temperature is 35-45 degrees Celsius for the hydrolysis of pNP-esters. Remains active even at 65 degrees Celsius (about 60% of maximum activity) (PubMed:30502092).
Optimum pH9.0
Familypetase_like

Structure

Source Experimental, PDB 6EQE
Resolution0.92 Å
Residues265
Cα RMSD to IsPETase0.00 Å

Active site

Catalytic triadSer160 · His237 · Asp206
Ser OG → His NE22.94 Å
His ND1 → Asp OD3.07 Å
Oxyanion donor 1161 (3.29 Å)
Oxyanion donor 287 (5.65 Å)
Cleft width21.27 Å
Cleft depth4.27 Å
Cleft residues83

Aromatic clamp: PHE201 · TRP159 · TRP185 · TYR219 · TYR87

Measured activity

ParameterValueSubstrateEvidenceSource
catalytic activity PET measured PMID 26965627 · PMID 29235460 · PMID 29374183 · PMID 29603535 · PMID 29666242 · PMID 32269349
(ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+)
km 0.048 mM pNP-octanoate measured PMID 30502092
km 0.053 mM pNP-hexanoate measured PMID 30502092
km 0.315 mM pNP-butanoate measured PMID 30502092
km 0.431 mM pNP-acetate measured PMID 30502092
km 2.283 mM pNP-dodecanoate measured PMID 30502092
performance claim PET from review 10.1126/science.aad6359
Wild type; weak on crystalline PET
ph opt 9.0 pH measured PMID 26965627 · PMID 29603535 · PMID 30502092
Optimum pH is 9 for PET film hydrolysis (PubMed:26965627). Optimum pH is 9 for PET (commercial drinking bottle) hydrolysis. Optimum pH is 6.5-8.0 for BHET hydrolysis (PubMed:29603535). Optimum pH is 8.0 for the hydrolysis of pNP-esters. The enzyme is active at pH 6-10, has an optimal pH range of 7-9 and it is rapidly inactivated below pH 7.0 or above pH 9.0 (PubMed:30502092).
topt 32.5 degC PET from review 10.1126/science.aad6359
Published as 30 to 35 °C. Midpoint stored in the numeric column; the published interval is this text.
topt 40.0 degC measured PMID 26965627 · PMID 29603535 · PMID 30502092
Optimum temperature is 40 degrees Celsius for PET film hydrolysis (PubMed:26965627). Optimum temperature is 30 degrees Celsius for PET (commercial drinking bottle) hydrolysis and BHET hydrolysis (PubMed:29603535). Optimum temperature is 35-45 degrees Celsius for the hydrolysis of pNP-esters. Remains active even at 65 degrees Celsius (about 60% of maximum activity) (PubMed:30502092).

Related in PANTS

Lineage

Variants built on this enzyme:
DepoPETaseDuraPETaseESTHER:P71505FAST-PETaseFAST-PETase-N212A/K233C/S282CHotPETaseIsPETase-W159H/S238FThermoPETaseZ1-PETase

Nearest metagenomic candidates

No candidate in the catalogue names this enzyme as its nearest match.

Identifiers and cross-references

Ideonella/Piscinibacter sakaiensis 201-F6. The reference PETase. 290 aa precursor; literature mutation numbering matches this precursor directly (verified: S160/D206/H237 triad, mobile W185).