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Information on EC 3.1.1.101 - poly(ethylene terephthalate) hydrolase
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EC Tree
3.1.1.101 poly(ethylene terephthalate) hydrolaseIUBMB Comments
The enzyme, isolated from the bacterium Ideonella sakaiensis, also produces small amounts of terephthalate (cf. EC 3.1.1.102, mono(ethylene terephthalate) hydrolase). The reaction takes place on PET-film placed in solution.
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Word Map
- 3.1.1.101
- sakaiensis
- ideonella
- degradation
-
polyester
- waste
-
film
-
terephthalic
- mhetase
-
mono2-hydroxyethyl
-
bottle
-
thermobifida
-
pet-degrading
- fusca
-
amorphous
- environmental protection
- cutinases
-
compost
-
thermoplastic
-
plastic-degrading
- analysis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
(ethylene terephthalate)n
+
=
(ethylene terephthalate)n-1
+
Synonyms
petase, tfcut2, poly(ethylene terephthalate) hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cut1
Cut2
cutinase 1
cut_1.KW3
ISF6_4831
PET hydrolase
PETase
Tcur_0390
Tcur_1278
TfCut2
PET hydrolase
-
-
-
-
PETase
-
-
-
-
PETase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(ethylene terephthalate)n + H2O = (ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
poly(ethylene terephthalate) hydrolase
The enzyme, isolated from the bacterium Ideonella sakaiensis, also produces small amounts of terephthalate (cf. EC 3.1.1.102, mono(ethylene terephthalate) hydrolase). The reaction takes place on PET-film placed in solution.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + mono(2-hydroxyethyl)terephthalic acid
(ethylene terephthalate)n + H2O
terephthalic acid + mono(2-hydroxyethyl)terephthalate + ?
hydrolysis of poly(ethylene terephthalate) (PET) is shown for all three enzymes (native Thc_Cut1 and two glycosylation site knockout mutants (Thc_Cut1_koAsn and Thc_Cut1_koST)) based on quantification of released products by HPLC and similar concentrations of released terephthalic acid (TPA) and mono(2-hydroxyethyl) terephthalate (MHET)
-
-
?
bis(2-hydroxyethyl) terephthalic acid + H2O
mono(2-hydroxyethyl)terephthalic acid + ethylene glycol
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
3-hydroxybutyric acid + ?
polyesters poly(butylene succinate) is hydrolyzed to significantly higher extent than poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
-
?
polyesters poly(butylene succinate) + H2O
succinic acid + 1,4-butanediol + ?
polyesters poly(butylene succinate) is hydrolyzed to significantly higher extent than poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
-
?
(epsilon-caprolactone)n + H2O
(epsilon-caprolactame)n-1 + ethylene terephthalate
-
-
-
?
(epsilon-caprolactone)n + H2O
(epsilon-caprolactame)n-1 + ethylene terephthalate
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Fusarium vanettenii DSM 62420
-
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
high flexibility of PETase loops at room temperature enables this enzyme to bind and degrade PET more efficiently than other cutinases
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
high flexibility of PETase loops at room temperature enables this enzyme to bind and degrade PET more efficiently than other cutinases
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
high flexibility of PETase loops at room temperature enables this enzyme to bind and degrade PET more efficiently than other cutinases
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
E5BBQ3
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
E5BBQ3
substrates are amorphous PET film or PET fibers
terephthalate is the dominant hydrolysis product detected after a reaction time of 50 h at 65°C. Monohydroxyethylene terephthalate which inhibits the hydrolysis of PET is almost completely converted into terephthalate and accounts for less than 9.1% of the total hydrolysis products
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
E5BBQ3
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
E5BBQ3
substrates are amorphous PET film or PET fibers
terephthalate is the dominant hydrolysis product detected after a reaction time of 50 h at 65°C. Monohydroxyethylene terephthalate which inhibits the hydrolysis of PET is almost completely converted into terephthalate and accounts for less than 9.1% of the total hydrolysis products
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
E5BBQ3
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + mono(2-hydroxyethyl)terephthalic acid
-
mono(2-hydroxyethyl)terephthalic acid is the major product, plus minor amounts of terephthalic acid and bis(2-hydroxyethyl) terephthalic acid
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + mono(2-hydroxyethyl)terephthalic acid
-
mono(2-hydroxyethyl)terephthalic acid is the major product, plus minor amounts of terephthalic acid and bis(2-hydroxyethyl) terephthalic acid
-
?
4-nitrophenyl acetate + H2O
acetate + 4-nitrophenol
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
?
bis(2-hydroxyethyl) terephthalic acid + H2O
mono(2-hydroxyethyl)terephthalic acid + ethylene glycol
-
enzyme does not catalyze further decomposition of mono(2-hydroxyethyl)terephthalic acid
-
?
bis(2-hydroxyethyl) terephthalic acid + H2O
mono(2-hydroxyethyl)terephthalic acid + ethylene glycol
-
enzyme does not catalyze further decomposition of mono(2-hydroxyethyl)terephthalic acid
-
?
additional information
?
-
enzyme shows low activity on 4-nitrophenyl aliphatic esters
-
-
?
additional information
?
-
enzyme shows low activity on 4-nitrophenyl aliphatic esters
-
-
?
additional information
?
-
E5BBQ3
analysis of the partially hydrolyzed PET nanoparticles provides indirect evidence for an endo-type hydrolytic mechanism of Cut2 in the heterogeneous degradation of aromatic polyesters
-
-
?
additional information
?
-
E5BBQ3
enzyme additionally catalyzes hydrolysis of ethylene terephthalate and bis(2-hydroxyethyl) terephthalic acid, reaction of EC 3.1.1.102
-
-
?
additional information
?
-
E5BBQ3
analysis of the partially hydrolyzed PET nanoparticles provides indirect evidence for an endo-type hydrolytic mechanism of Cut2 in the heterogeneous degradation of aromatic polyesters
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Ca2+
E5BBQ2, E5BBQ3
and Mg2+, presence of 10 mM each increases thermostability by about 10 degrees. Residues Asp174, Asp204, and Glu253 are potential binding residues for the two cations
Mg2+
E5BBQ2, E5BBQ3
and Ca2+, presence of 10 mM each increases thermostability by about 10 degrees. Residues Asp174, Asp204, and Glu253 are potential binding residues for the two cations
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bis(2-hydroxyethyl) terephthalic acid
E5BBQ3
competitive inhibition of the hydrolytic activity against PET nanoparticles
ethylene terephthalate
E5BBQ3
competitive inhibition of the hydrolytic activity against PET nanoparticles
PMSF
E5BBQ3
the PMSF protein complex reveals covalent modification of S130 and binding of one of the oxygens of the tetrahedral adduct in the oxyanion hole formed by the main chain nitrogens of M131 and Y60
MOPS
E5BBQ3
hydrolytic activity against PET films is strongly influenced by the reaction medium buffers tris(hydroxymethyl)aminomethane (Tris), 3-(N-morpholino)propanesulfonic acid (MOPS), and sodium phosphate. MOPS acts as a competitive inhibitor
MOPS
hydrolytic activity against PET films is strongly influenced by the reaction medium buffers tris(hydroxymethyl)aminomethane (Tris), 3-(N-morpholino)propanesulfonic acid (MOPS), and sodium phosphate. At a MOPS concentration of 1 M, the hydrolysis rate decreases by 90%. MOPS acts as a competitive inhibitor
Tris
E5BBQ3
hydrolytic activity against PET films is strongly influenced by the reaction medium buffers tris(hydroxymethyl)aminomethane (Tris), 3-(N-morpholino)propanesulfonic acid (MOPS), and sodium phosphate. At a Tris concentration of 1 M, the hydrolysis rate decreases by about 80%. Tris acts as a competitive inhibitor
Tris
hydrolytic activity against PET films is strongly influenced by the reaction medium buffers tris(hydroxymethyl)aminomethane (Tris), 3-(N-morpholino)propanesulfonic acid (MOPS), and sodium phosphate. At a Tris concentration of 1 M, the hydrolysis rate decreases by more than 90%. Tris acts as a competitive inhibitor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
additional information
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
additional information
E5BBQ3
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
additional information
E9LVI0
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
additional information
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
additional information
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
additional information
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
additional information
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
additional information
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
additional information
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
additional information
-
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
-