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Information on EC 3.1.1.101 - poly(ethylene terephthalate) hydrolase
for references in articles please use BRENDA:EC3.1.1.101
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.1 Carboxylic-ester hydrolases
3.1.1.101 poly(ethylene terephthalate) hydrolase
IUBMB 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.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 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
Reaction Schemes
show(ethylene terephthalate)n
+
=
(ethylene terephthalate)n-1
+
Synonyms
petase, tfcut2, poly(ethylene terephthalate) hydrolase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cut1
Cut2
cutinase 1
cutinase-type poly(ethylene terephthalate) hydrolase
cut_1.KW3
ETase
ISF6_4831
IsPETase
MHET hydrolase
MHETase
monohydroxyethyl terephthalate hydrolase
MtCut
PET hydrolase
PET hydrolase Cut190
PET hydrolases
PET-hydrolase
PETase
PIsPETase
polyethylene terephthalate hydrolase
Tcur_0390
Tcur_1278
TfCut2
Thc_Cut2
additional information
cutinase-type poly(ethylene terephthalate) hydrolase
-
cutinase-type poly(ethylene terephthalate) hydrolase
-
-
IsPETase
-
PET hydrolase
-
-
-
-
PET hydrolase
-
PETase
-
-
-
-
PETase
-
polyethylene terephthalate hydrolase
-
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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
MetaCyc
polyethylene terephthalate degradation
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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
LITERATURE
COMMENTARY
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
bis(2-hydroxyethyl) terephthalate
-
Substrates: the concentration and the proportion (molar ratio) of hydrolysis products, terephthalic acid (TPA), mono(2-hydroxyethyl) terephthalate (MHET), and bis(2-hydroxyethyl) terephthalate (BHET), are significantly changed depending on the reaction temperature. The TPA released at 70°C is 3.65fold higher than at 50°C. At higher temperatures, the conversion of MHET into TPA is favored. The enzymatic PET hydrolysis by HiC is very sensitive to the enzyme concentration, indicating that it strongly adsorbs on the polymer surface. The concentration of TPA, MHET, and BHET increases as the enzyme concentration increased, and a maximum is achieved using 40-50 vol % of HiC
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
mono(2-hydroxyethyl) terephthalate
-
Substrates: the concentration and the proportion (molar ratio) of hydrolysis products, terephthalic acid (TPA), mono(2-hydroxyethyl) terephthalate (MHET), and bis(2-hydroxyethyl) terephthalate (BHET), are significantly changed depending on the reaction temperature. The TPA released at 70°C is 3.65fold higher than at 50°C. At higher temperatures, the conversion of MHET into TPA is favored. The enzymatic PET hydrolysis by HiC is very sensitive to the enzyme concentration, indicating that it strongly adsorbs on the polymer surface. The concentration of TPA, MHET, and BHET increases as the enzyme concentration increased, and a maximum is achieved using 40-50 vol % of HiC
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
terephthalic acid
-
Substrates: the concentration and the proportion (molar ratio) of hydrolysis products, terephthalic acid (TPA), mono(2-hydroxyethyl) terephthalate (MHET), and bis(2-hydroxyethyl) terephthalate (BHET), are significantly changed depending on the reaction temperature. The TPA released at 70°C is 3.65fold higher than at 50°C. At higher temperatures, the conversion of MHET into TPA is favored. The enzymatic PET hydrolysis by HiC is very sensitive to the enzyme concentration, indicating that it strongly adsorbs on the polymer surface. The concentration of TPA, MHET, and BHET increases as the enzyme concentration increased, and a maximum is achieved using 40-50 vol % of HiC
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
terephthalic acid + mono(2-hydroxyethyl)terephthalate + ?
Substrates: 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)
Products: -
Products: -
?
bis(2-hydroxyethyl) terephthalic acid + H2O
mono(2-hydroxyethyl)terephthalic acid + ethylene glycol
bis-((2-hydroxyethyl)terephthalic acid) + H2O
mono-(2-hydroxyethyl)terephthalic acid + terephthalic acid
Substrates: -
Products: -
Products: -
?
mono-(2-hydroxyethyl)terephthalic acid + H2O
2-hydroxyethanol + terephthalic acid
Substrates: -
Products: -
Products: -
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
3-hydroxybutyric acid + ?
Substrates: polyesters poly(butylene succinate) is hydrolyzed to significantly higher extent than poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
Products: -
Products: -
?
polyesters poly(butylene succinate) + H2O
succinic acid + 1,4-butanediol + ?
Substrates: polyesters poly(butylene succinate) is hydrolyzed to significantly higher extent than poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
Products: -
Products: -
?
polyethylene terephthalate + H2O
mono-(2-hydroxyethyl)terephthalate + terephthalic acid
Substrates: -
Products: -
Products: -
?
(epsilon-caprolactone)n + H2O
(epsilon-caprolactame)n-1 + ethylene terephthalate
Substrates: -
Products: -
Products: -
?
(epsilon-caprolactone)n + H2O
(epsilon-caprolactame)n-1 + ethylene terephthalate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: 4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
A0A2H5Z9R5
Substrates: highly active on the PET powder. Highest conversion occurrs at 70°C, at which 6.3 mM degradation products consisting of 0.17 mM bis(2-hydroxyethyl)terephthalate, 3.66 mM mono(hydroxyethyl) terephthalate and 2.47 mM terephthalic acid are generated by the enzyme (BhrPETase) after 20 h
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: 4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
A0A1F4JXW8
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
A0A1F4JXW8
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: PET hydrolysis activity on amorphous PET film
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: the variant N109A/V129T/A155R/L180C/R198K/A202C/R242C/S291C/G196T almost completely decomposes both transparent and colored post-consumer PET powder at 55°C within half a day in a pH-stat bioreactor
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: 4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Fusarium vanettenii DSM 62420
-
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
A0A1H6AD45
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
A0A3L8BW54
Substrates: PET hydrolysis activity on amorphous PET film
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: microparticle poly(ethylene terephthalate). The enzyme generates mono (2-hydroxyethyl) terephthalic acid and terephthalic acid as main products in equal quantities
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: PET hydrolysis activity on amorphous PET film
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Marinactinospora thermotolerans DSM 45145
Substrates: PET hydrolysis activity on amorphous PET film
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: microparticle poly(ethylene terephthalate). The enzyme generates mono (2-hydroxyethyl) terephthalic acid and terephthalic acid as main products in equal quantities
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
A0A3D5ATI9
Substrates: PET hydrolysis activity on amorphous PET film
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: 4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: 4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
E9UPM2
Substrates: PET hydrolysis activity on amorphous PET film
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: high flexibility of PETase loops at room temperature enables this enzyme to bind and degrade PET more efficiently than other cutinases
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: high flexibility of PETase loops at room temperature enables this enzyme to bind and degrade PET more efficiently than other cutinases
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: modeling of PET hydrolysis shows that the ability to hydrolyze internal bonds in the polymer (endo-lytic activity) is a key parameter for overall enzyme performance. Endo-lytic activity promotes the release of soluble PET fragments with two or three aromatic rings, which, in turn, are broken down with remarkable efficiency in the aqueous bulk
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: the biodegradability of various PET substrates depends on both their chemical structure and physical properties, including polymer length, crystallinity, glass transition temperature, surface area, and surface charge
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: the enzyme act on low crystal PET films
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: PETase enzyme synthesised in the chloroplast of the microalga Chlamydomonas reinhardtii is active against post-consumer plastics
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: both soluble and insoluble PET fragments are consistently hydrolyzed much faster than intact PET
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: the enzyme generates mono (2-hydroxyethyl) terephthalic acid (MEHT) and terephthalic acid (TPA) as main products, with higher MHET to TPA ratio
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: the enzyme (MHETase, cf. EC 3.1.1.102) also hydrolyzes 4-[(2-hydroxyethoxy)carbonyl]benzoate and bis(2-hydroxyethyl) terephthalate
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Piscinibacter sakaiensis 201-F6
Substrates: high flexibility of PETase loops at room temperature enables this enzyme to bind and degrade PET more efficiently than other cutinases
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Piscinibacter sakaiensis 201-F6
Substrates: modeling of PET hydrolysis shows that the ability to hydrolyze internal bonds in the polymer (endo-lytic activity) is a key parameter for overall enzyme performance. Endo-lytic activity promotes the release of soluble PET fragments with two or three aromatic rings, which, in turn, are broken down with remarkable efficiency in the aqueous bulk
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Piscinibacter sakaiensis 201-F6
Substrates: the biodegradability of various PET substrates depends on both their chemical structure and physical properties, including polymer length, crystallinity, glass transition temperature, surface area, and surface charge
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Piscinibacter sakaiensis 201-F6
Substrates: the enzyme act on low crystal PET films
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Piscinibacter sakaiensis 201-F6
Substrates: the enzyme generates mono (2-hydroxyethyl) terephthalic acid (MEHT) and terephthalic acid (TPA) as main products, with higher MHET to TPA ratio
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Piscinibacter sakaiensis 201-F6
Substrates: the enzyme (MHETase, cf. EC 3.1.1.102) also hydrolyzes 4-[(2-hydroxyethoxy)carbonyl]benzoate and bis(2-hydroxyethyl) terephthalate
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: PETase enzyme synthesised in the chloroplast of the microalga Chlamydomonas reinhardtii is active against post-consumer plastics
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: 4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: 4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: 4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: 4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Saccharomonospora viridis AHK190
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: PET hydrolysis activity on amorphous PET film
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: 4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: PET hydrolysis activity on amorphous PET film
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: PET hydrolysis activity on amorphous PET film
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: PET hydrolysis activity on amorphous PET film
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
E5BBQ3
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
E5BBQ3
Substrates: substrates are amorphous PET film or PET fibers
Products: 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
Products: 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
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Q6A0I4, WP_104613137.1
Substrates: PET hydrolysis activity on amorphous PET film
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
E5BBQ3
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
E5BBQ3
Substrates: substrates are amorphous PET film or PET fibers
Products: 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
Products: 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
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: 4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: 4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + ethylene terephthalate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + ethylene terephthalate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + mono(2-hydroxyethyl)terephthalic acid
Substrates: -
Products: mono(2-hydroxyethyl)terephthalic acid is the major product, plus minor amounts of terephthalic acid and bis(2-hydroxyethyl) terephthalic acid
Products: 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
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: mono(2-hydroxyethyl)terephthalic acid is the major product, plus minor amounts of terephthalic acid and bis(2-hydroxyethyl) terephthalic acid
Products: 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
4-nitrophenol + acetate
A0A2H5Z9R5
Substrates: -
Products: -
Products: -
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: -
Products: -
?
4-nitrophenyl acetate + H2O
acetate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenyl acetate + H2O
acetate + 4-nitrophenol
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: -
Products: -
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
A0A2H5Z9R5
Substrates: -
Products: -
Products: -
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
Fusarium vanettenii DSM 62420
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: -
Products: -
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
A0A2H5Z9R5
Substrates: -
Products: -
Products: -
?
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl hexadecanoate + H2O
4-nitrophenol + hexadecanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl hexadecanoate + H2O
4-nitrophenol + hexadecanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
A0A2H5Z9R5
Substrates: -
Products: -
Products: -
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: -
Products: -
?
4-nitrophenyl octadecanoate + H2O
4-nitrophenol + octadecanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl octadecanoate + H2O
4-nitrophenol + octadecanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
A0A2H5Z9R5
Substrates: -
Products: -
Products: -
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: -
Products: -
?
4-nitrophenyl tetradecanoate + H2O
4-nitrophenol + tetradecanoate
A0A2H5Z9R5
Substrates: -
Products: -
Products: -
?
4-nitrophenyl tetradecanoate + H2O
4-nitrophenol + tetradecanoate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl tetradecanoate + H2O
4-nitrophenol + tetradecanoate
Substrates: -
Products: -
Products: -
?
bis (2-hydroxyethyl) terephthalic acid + H2O
?
Substrates: -
Products: -
Products: -
?
bis (2-hydroxyethyl) terephthalic acid + H2O
?
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: -
Products: -
?
bis(2-hydroxyethyl) terephthalic acid + H2O
?
Substrates: -
Products: -
Products: -
?
bis(2-hydroxyethyl) terephthalic acid + H2O
?
Substrates: -
Products: -
Products: -
?
bis(2-hydroxyethyl) terephthalic acid + H2O
mono(2-hydroxyethyl)terephthalic acid + ethylene glycol
Substrates: -
Products: enzyme does not catalyze further decomposition of mono(2-hydroxyethyl)terephthalic acid
Products: 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
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: enzyme does not catalyze further decomposition of mono(2-hydroxyethyl)terephthalic acid
Products: enzyme does not catalyze further decomposition of mono(2-hydroxyethyl)terephthalic acid
?
bis(2-hydroxyethyl)terephthalate + H2O
?
A0A2H5Z9R5
Substrates: -
Products: -
Products: -
?
bis(2-hydroxyethyl)terephthalate + H2O
?
Substrates: -
Products: -
Products: -
?
mono (2-hydroxyethyl) terephthalic acid + H2O
?
Substrates: -
Products: -
Products: -
?
mono (2-hydroxyethyl) terephthalic acid + H2O
?
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: -
Products: -
?
mono(2-hydroxyethyl) terephthalic acid + H2O
?
Substrates: -
Products: -
Products: -
?
mono(2-hydroxyethyl) terephthalic acid + H2O
?
Substrates: -
Products: -
Products: -
?
polyethylene-2,5-furandicarboxylate + H2O
?
Substrates: -
Products: -
Products: -
?
polyethylene-2,5-furandicarboxylate + H2O
?
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme shows low activity on 4-nitrophenyl aliphatic esters
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with 4-nitrophenyl dodecanoate or 4-nitrophenyl tetradecanoate
Products: -
Products: -
-
additional information
?
-
Piscinibacter sakaiensis 201-F6
Substrates: enzyme shows low activity on 4-nitrophenyl aliphatic esters
Products: -
Products: -
?
additional information
?
-
E5BBQ3
Substrates: 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
Products: -
Products: -
?
additional information
?
-
E5BBQ3
Substrates: enzyme additionally catalyzes hydrolysis of ethylene terephthalate and bis(2-hydroxyethyl) terephthalic acid, reaction of EC 3.1.1.102
Products: -
Products: -
?
additional information
?
-
E5BBQ3
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Piscinibacter sakaiensis 201-F6
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Saccharomonospora viridis AHK190
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + ethylene terephthalate
Substrates: -
Products: -
Products: -
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + ethylene terephthalate
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Ca2+
activity towards 4-nitrophenyl butanoate or poly(ethylene terephthalate) increases with increasing Ca2+ concentration. PET hydrolysis is maximum at 10-100 mM CaCl2 and decreases at higher Ca2+ concentrations
Ca2+
improves enzyme activity and thermal stability, overview
Ca2+
E5BBQ3, E5BBQ2
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+
E5BBQ3, E5BBQ2
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
additional information
no inhibition by mono-(2-hydroxyethyl)terephthalic acid
-
additional information
-
the enzyme seems not to be inhibited by any of the main PET hydrolysis products such as terephthalic acid, mono-(2-hydroxyethyl) terephthalate, and bis-(2-hydroxyethyl) terephthalate
-
additional information
enzyme concentration-dependent inhibition. The concentration-dependent inhibition is a surface phenomenon produced when enzyme molecules interact with each other following substrate binding
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hydrophobin RolA
the rate of PETase hydrolysis can be significantly increased in the presence of hydrophobin RolA. The hydrolysis of PET bottle by RolA-PETase achieves the highest weight loss of 26% in 4 days
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.48
bis (2-hydroxyethyl) terephthalic acid
pH 8.5, 40°C
4.27
bis(2-hydroxyethyl) terephthalic acid
pH 8.5, 40°C
3.07
bis-((2-hydroxyethyl)terephthalic acid)
pH 8.0, 40°C, recombinant wild-type enzyme
0.72
mono (2-hydroxyethyl) terephthalic acid
pH 8.5, 40°C
0.13
mono(2-hydroxyethyl) terephthalic acid
pH 8.5, 40°C
0.75
mono-(2-hydroxyethyl)terephthalic acid
pH 8.0, 40°C, recombinant wild-type enzyme
additional information
additional information
-
comparative kinetic analysis with respect to activity on both polymeric PET and smaller (soluble or insoluble) model substrates, primarily PET fragments
-
additional information
additional information
Michaelis-Menten kinetics and modelling
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.95
bis (2-hydroxyethyl) terephthalic acid
pH 8.5, 40°C
3.07
bis(2-hydroxyethyl) terephthalic acid
pH 8.5, 40°C
4.27
bis-((2-hydroxyethyl)terephthalic acid)
pH 8.0, 40°C, recombinant wild-type enzyme
0.14
mono (2-hydroxyethyl) terephthalic acid
pH 8.5, 40°C
0.75
mono(2-hydroxyethyl) terephthalic acid
pH 8.5, 40°C
0.13
mono-(2-hydroxyethyl)terephthalic acid
pH 8.0, 40°C, recombinant wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.33
bis (2-hydroxyethyl) terephthalic acid
pH 8.5, 40°C
1.41
bis(2-hydroxyethyl) terephthalic acid
pH 8.5, 40°C
1.39
bis-((2-hydroxyethyl)terephthalic acid)
pH 8.0, 40°C, recombinant wild-type enzyme
0.019
mono (2-hydroxyethyl) terephthalic acid
pH 8.5, 40°C
0.176
mono(2-hydroxyethyl) terephthalic acid
pH 8.5, 40°C
0.173
mono-(2-hydroxyethyl)terephthalic acid
pH 8.0, 40°C, recombinant wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
87.9
substrate: bis(2-hydroxyethyl)terephthalate, pH 8.0, 40°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
over 40% of maximal activity within this range
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
hydrolysis of 4-nitrophenyl butanoate, without CaCl2
40
50
55
60
70
40
hydrolysis of 4-nitrophenyl butanoate, in presence of 1 mM CaCl2
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
30°C: about 25% of maximal activity, 50°C: about 35% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
dienelactone hydrolase-domain containing protein
A0A1F4JXW8
UniProt
brenda
-
A0A1F4JXW8
UniProt
brenda
dienelactone hydrolase domain-containing protein
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
A0A1F4JXW8
BbPETase is an enzyme in the evolution of efficient PET degradation
physiological function
additional information
physiological function
MtCut is a cutinase-type PET-degrading enzyme, which exhibits efficient PET-hydrolyzing activity at the ambient temperatures. MtCut performs PET hydrolysis in an exo-type manner. The cutinase activity of MtCut toward pNP esters is similar in substrate selectivity and catalytic efficiency to reported cutinases (EC 3.1.1.74) are more active on pNP-C6 or C8 than C2 or long-chain fatty acid esters. Enzyme MtCut efficiently transforms polyethylene terephthalate (PET) into mono-(2-hydroxyethyl) terephthalic acid (MHET) and terephthalic acid (TPA) at ambient temperatures, with no significant inhibitory effects from hydrolysis products
physiological function
MHETase plays several roles in the biodegradation of poly(ethylene terephthalate) using the bis(2-hydroxyethyl) terephthalate hydrolase and exo-PETase activities as well as the 4-[(2-hydroxyethoxy)carbonyl]benzoate (MHET) hydrolysis function
physiological function
Piscinibacter sakaiensis 201-F6
-
MHETase plays several roles in the biodegradation of poly(ethylene terephthalate) using the bis(2-hydroxyethyl) terephthalate hydrolase and exo-PETase activities as well as the 4-[(2-hydroxyethoxy)carbonyl]benzoate (MHET) hydrolysis function
-
physiological function
-
MtCut is a cutinase-type PET-degrading enzyme, which exhibits efficient PET-hydrolyzing activity at the ambient temperatures. MtCut performs PET hydrolysis in an exo-type manner. The cutinase activity of MtCut toward pNP esters is similar in substrate selectivity and catalytic efficiency to reported cutinases (EC 3.1.1.74) are more active on pNP-C6 or C8 than C2 or long-chain fatty acid esters. Enzyme MtCut efficiently transforms polyethylene terephthalate (PET) into mono-(2-hydroxyethyl) terephthalic acid (MHET) and terephthalic acid (TPA) at ambient temperatures, with no significant inhibitory effects from hydrolysis products
-
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
C3RYL0
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
the enzyme contains MtCut contains a conserved pentapeptide sequence motif (GHSMG), and a catalytic triad (Ser178-Asp224-His256). Molecular docking and molecular dynamics simulations
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
-
the enzyme contains MtCut contains a conserved pentapeptide sequence motif (GHSMG), and a catalytic triad (Ser178-Asp224-His256). Molecular docking and molecular dynamics simulations
-
Show AA Sequence and Transmembrane Helices (258 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 34000, recombinant His-tagged enzyme, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
0.92 A resolution X-ray crystal structure reveals features common to both cutinases and lipases. PETase retains the ancestral alpha/beta-hydrolase fold but exhibits a more open active-site cleft than homologous cutinases
crystal structures of the secreted enzyme in its apo form and in a complex with BHET and with the MHET covalent intermediate
hanging-drop vapor-diffusion technique at 20°C. Crystal structure of PETase at 1.5 A resolution. The enzyme has a Ser-His-Asp catalytic triad at its active site and contains an optimal substrate binding site to accommodate four monohydroxyethyl terephthalate moieties of PET. Based on structural and site-directed mutagenesis experiments, the detailed process of PET degradation into MHET, terephthalic acid, and ethylene glycol is suggested
sitting drop vapor diffusion method at 4°C with a mixture at a 1:1 ratio of protein and reservoir solution. Crystal structure of PETase is determined at 2.02 A resolution and employed in molecular dynamics simulations showing that the active site of PETase has higher flexibility at room temperature than its thermophilic counterparts. This flexibility is controlled by a novel disulfide bond in its active site, with its removal leading to destabilization of the catalytic triad and reduction of the hydrolase activity. High flexibility of PETase loops at room temperature enables this enzyme to bind and degrade PET more efficiently than other cutinases
sitting-drop vapor-diffusion method at 25°C, crystallized in the orthorhombic space group P212121. The structure is solved at 1.58 A resolution
molecular replacement with a poly-Ala model of Streptomyces exofoliatus lipase, PDB-ID: 1JFR, in free as well as in inhibitor-bound form. The enzyme forms a classical alpha/beta-hydrolase fold with a central nine-stranded beta-sheet flanked by 11 alpha-helices on both sides. The catalytic triad, comprising S130, D176 and H208, is located in a crevice on the surface of the enzyme
E5BBQ3
structural model generated on the basis of PDB ID 3VIS. The polyester hydrolase reveals a typical alpha/beta hydrolase fold. The catalytic triad formed by residues S130, D176 and H208 is exposed to the solvent
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A209C/R283C/N364C/D418C
A0A1F4JXW8
the activity is significantly lower than that of N364C/D418C variant. The expression level of the variant is extremely low
A99R
A0A1F4JXW8
variant exhibits increased activities in comparison to that of wild-type enzyme
N364C/D418C
A0A1F4JXW8
the variant exhibits approximately an 11fold increase over the wild-type enzyme (BbPETaseCD, core domain of the enzyme) in the long-term (14 days) degradation of PET films. The melting temperature (Tm) of the N364C/D418C variant presents an increase of 14.8°C over that of wild-type (56.5°C)
P207C/D280C/N364C/D418C
A0A1F4JXW8
the variant shows increased activity, the activity is significantly lower than that of N364C/D418C variant. The expression level of the variant is extremely low
S174R
A0A1F4JXW8
variant exhibits increased activities in comparison to that of wild-type enzyme
S335N/T338I/M363I/N365G
A0A1F4JXW8
variant with an enhanced PET-degrading activity and thermal stability
T397R
A0A1F4JXW8
variant exhibits increased activities in comparison to that of wild-type enzyme
L61T
-
activity is improved towards bis(2-hydroxyethyl) terephthalic acid
L61T/W132H/R259A
-
mutant with the highest catalytic efficiency towards PET film
A155R
Tm-value is 0.41°C higher than wild-type value
F101Y
Tm-value is 1.03°C higher than wild-type value
G196L
Tm-value is 0.53°C higher than wild-type value
G196T
Tm-value is 4.52°C higher than wild-type value
G76C/A143C
Tm-value is 3.15°C lower than wild-type value
L180C/A202C
Tm-value is 2.67°C higher than wild-type value
N109A
Tm-value is 3.18°C higher than wild-type value
N109A/V129T/A155R/L180C/R198K/A202C/R242C/S291C/G196T
variant with disulfide bonds between L180C/A202C and R242C/S291C. The variant exhibits robust thermostability with a Tm of 83.2°C and 41.7fold enhanced PET hydrolytic activity at 60°C compared with wild-type enzyme. The variant almost completely decomposes both transparent and colored post-consumer PET powder at 55°C within half a day in a pH-stat bioreactor
N195H
Tm-value is 1.13°C higher than wild-type value
P136S
Tm-value is 1.24°C higher than wild-type value
Q107S
Tm-value is 0.82°C higher than wild-type value
R151A
Tm-value is 0.11°C higher than wild-type value
R198K
Tm-value is 1.85°C higher than wild-type value
R242C/S291C
Tm-value is 3.07°C higher than wild-type value
T204C/R233C
Tm-value is 3.98°C lower than wild-type value
V129T
Tm-value is 2.67°C higher than wild-type value
V217I
Tm-value is 1.34°C higher than wild-type value
F250A
-
could hydrolyze bis(2-hydroxyethyl) terephthalate better than wild-type enzyme MG8 (about 3fold higher combined product output), but its PET hydrolysis efficiency remains similar to the wild-type enzyme
A180I
mutation results in more space on the binding center and higher activity than the wild-type enzyme
A226V
2.9fold increase in activity as compared to wild-type enzyme
C174S
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to less than 5% compared to wild-type value
C210S
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is is abolished
D220N
2.5fold increase in activity as compared to wild-type enzyme
F424I
the variant shows 3.4times increased MHETase activity in comparison with wild-type enzyme
F424N
the variant shows 3.9times increased MHETase activity in comparison with wild-type enzyme
F424V
the variant shows 3.0times increased MHETase activity in comparison with wild-type enzyme
I139R
variant with the highest Tm value of 56.4°C and 3.6times higher PET degradation activity than the wild-type enzyme
I179A
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 15% compared to wild-type value
I179F
-
enzymatic activity of the mutant enzyme exhibits 2.5fold increase in comparison with wild-type PETase
L88F
-
enzymatic activity of the mutant enzyme exhibits 2.1fold increase in comparison with wild-type PETase
M132A
R260H
1.3fold increase in activity as compared to wild-type enzyme
R411K
the variant shows 1.7times increased MHETase activity in comparison with wild-type enzyme
R411K/F424I
R411K/F424N
the variant shows 8.7times increased MHETase activity in comparison with wild-type enzyme
R411K/F424V
R411K/S416A/F424I
R61A
-
enzymatic activity of the mutant enzyme exhibits 1.4fold increase in comparison with wild-type PETase
S121E/D186H/R280A
enhanced thermostability, decrease in concentration-dependent inhibition
S131A
S139T
mutant with higher PET film degradation activity than wild-type activity. The amount of degradation product terephthalic acid is 8% higher than that of wild-type enzyme
S185H
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 45% compared to wild-type value
S238F/W159H
the mutant enzyme adopts a more productive interaction with PET
S242T
4.9fold increase in activity as compared to wild-type enzyme
S92K/D157E/R251A
the variant exhibits higher thermostability but also shows a 1.74fold kcat increase towards mono-(2-hydroxyethyl) terephthalate, which achieved PET depolymerization to complete monomer terephthalic acid
T151I
1.3fold increase in activity as compared to wild-type enzyme
T59A
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 95% compared to wild-type value
V107I
1.6fold increase in activity as compared to wild-type enzyme
V52I/A209T/S223T
1.6fold increase in activity as compared to wild-type enzyme
W130A
W130H
W156A
W159H/S238F
enhanced thermostability, decrease in concentration-dependent inhibition
Y58A
C174S
Piscinibacter sakaiensis 201-F6
-
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to less than 5% compared to wild-type value
-
C210S
Piscinibacter sakaiensis 201-F6
-
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is is abolished
-
D220N
Piscinibacter sakaiensis 201-F6
-
2.5fold increase in activity as compared to wild-type enzyme
-
F424I
Piscinibacter sakaiensis 201-F6
-
the variant shows 3.4times increased MHETase activity in comparison with wild-type enzyme
-
F424N
Piscinibacter sakaiensis 201-F6
-
the variant shows 3.9times increased MHETase activity in comparison with wild-type enzyme
-
F424V
Piscinibacter sakaiensis 201-F6
-
the variant shows 3.0times increased MHETase activity in comparison with wild-type enzyme
-
I139R
Piscinibacter sakaiensis 201-F6
-
variant with the highest Tm value of 56.4°C and 3.6times higher PET degradation activity than the wild-type enzyme
-
R260H
Piscinibacter sakaiensis 201-F6
-
1.3fold increase in activity as compared to wild-type enzyme
-
R411K
Piscinibacter sakaiensis 201-F6
-
the variant shows 1.7times increased MHETase activity in comparison with wild-type enzyme
-
R411K/F424N
Piscinibacter sakaiensis 201-F6
-
the variant shows 8.7times increased MHETase activity in comparison with wild-type enzyme
-
S121E/D186H/R280A
Piscinibacter sakaiensis 201-F6
-
enhanced thermostability, decrease in concentration-dependent inhibition
-
S131A
S139T
Piscinibacter sakaiensis 201-F6
-
mutant with higher PET film degradation activity than wild-type activity. The amount of degradation product terephthalic acid is 8% higher than that of wild-type enzyme
-
S185H
Piscinibacter sakaiensis 201-F6
-
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 45% compared to wild-type value
-
S238F/W159H
Piscinibacter sakaiensis 201-F6
-
the mutant enzyme adopts a more productive interaction with PET
-
S242T
Piscinibacter sakaiensis 201-F6
-
4.9fold increase in activity as compared to wild-type enzyme
-
S92K/D157E/R251A
Piscinibacter sakaiensis 201-F6
-
the variant exhibits higher thermostability but also shows a 1.74fold kcat increase towards mono-(2-hydroxyethyl) terephthalate, which achieved PET depolymerization to complete monomer terephthalic acid
-
V107I
Piscinibacter sakaiensis 201-F6
-
1.6fold increase in activity as compared to wild-type enzyme
-
V52I/A209T/S223T
Piscinibacter sakaiensis 201-F6
-
1.6fold increase in activity as compared to wild-type enzyme
-
W156A
Piscinibacter sakaiensis 201-F6
-
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 10% compared to wild-type value
-
W159H/S238F
Piscinibacter sakaiensis 201-F6
-
enhanced thermostability, decrease in concentration-dependent inhibition
-
L136F/Q138A/S226P/R228S/D250C/E296C/Q123H/N202H/K305del/L306del/N307del
the best performing Cut190 variant produces more than 90 mM degradation products at 63°C in 3 days and approximately 80 mM at 65°C in one day, using amorphous PET powders
Q138A/D250C/E296C/Q123H/N202H
mutation results in an increased Tm
S226P/R228S
5 °C increase in Tm with 300 mM CaCl2 and 24% glycerol, enhancing the activity and yield of terephtalic acid, at 63°C
L136F/Q138A/S226P/R228S/D250C/E296C/Q123H/N202H/K305del/L306del/N307del
Saccharomonospora viridis AHK190
-
the best performing Cut190 variant produces more than 90 mM degradation products at 63°C in 3 days and approximately 80 mM at 65°C in one day, using amorphous PET powders
-
F243I/D238C/S283C/Y127G
improved activity, and increased Tm value by 9.3°C
F243W/D238C/S283C/Y127G
improved activity, and increased Tm value by 13.4°C
G63A/F210I/D205C7E254C/Q93G
variant with improved performance
R29N/A30V
the variant releases TPA at a higher level than the wild-type enzyme
F243I/D238C/S283C/Y127G
-
improved activity, and increased Tm value by 9.3°C
-
F243W/D238C/S283C/Y127G
-
improved activity, and increased Tm value by 13.4°C
-
G63A/F210I/D205C7E254C/Q93G
-
variant with improved performance
-
R29N/A30V
-
the variant releases TPA at a higher level than the wild-type enzyme
-
D174C/D253C
E5BBQ3
increase in melting temperature in absence and in presence of Ca2+
D204C/E253C/D174R
E5BBQ3
increase in temperature optimum to 75-80°C, mutant causes a weight loss of PET films of 25.0% at 70 °C after a reaction time of 48 h, compared to 0.3% for wild-type
D204R
E5BBQ3, E5BBQ2
mutation in residue involved in metal ion binding. Increase in melting point by 14 degrees compared to wild-type. Presence of 10 mM CaCl2 does not result in a considerable increase in melting point
E253R
E5BBQ3, E5BBQ2
mutation in residue involved in metal ion binding. Increase in melting point by 14 degrees compared to wild-type. Presence of 10 mM CaCl2 does not result in a considerable increase in melting point
G62A
E5BBQ3
exchange of amino acid residues of TfCut2 involved in substrate binding with those present in LC-cutinase, UniProt ID G9BY57, from an uncultured bacterium, leads to enzyme variants with increased PET hydrolytic activity at 65°C. Variant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme. Mutant G62A reveals a 5.5fold lower binding constant to the inhibitor mono-(2-hydroxyethyl) terephthalate than the wild type enzyme
G62A/I213S
E5BBQ3
exchange of amino acid residues of TfCut2 involved in substrate binding with those present in LC-cutinase, UniProt ID G9BY57, from an uncultured bacterium, leads to enzyme variants with increased PET hydrolytic activity at 65°C. Variant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme
H184S/Q92G/F209I/I213K
the variant exhibits 30fold more activity against PET than the wild-type enzyme
D174C/D253C
-
increase in melting temperature in absence and in presence of Ca2+
-
D204C/E253C/D174R
-
increase in temperature optimum to 75-80°C, mutant causes a weight loss of PET films of 25.0% at 70 °C after a reaction time of 48 h, compared to 0.3% for wild-type
-
D204R
-
mutation in residue involved in metal ion binding. Increase in melting point by 14 degrees compared to wild-type. Presence of 10 mM CaCl2 does not result in a considerable increase in melting point
-
E253R
-
mutation in residue involved in metal ion binding. Increase in melting point by 14 degrees compared to wild-type. Presence of 10 mM CaCl2 does not result in a considerable increase in melting point
-
G62A
-
exchange of amino acid residues of TfCut2 involved in substrate binding with those present in LC-cutinase, UniProt ID G9BY57, from an uncultured bacterium, leads to enzyme variants with increased PET hydrolytic activity at 65°C. Variant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme. Mutant G62A reveals a 5.5fold lower binding constant to the inhibitor mono-(2-hydroxyethyl) terephthalate than the wild type enzyme
-
G62A/I213S
-
exchange of amino acid residues of TfCut2 involved in substrate binding with those present in LC-cutinase, UniProt ID G9BY57, from an uncultured bacterium, leads to enzyme variants with increased PET hydrolytic activity at 65°C. Variant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme
-
additional information
M132A
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 15% compared to wild-type value
R411K/F424I
the variant shows 11.1times increased MHETase activity in comparison with wild-type enzyme
R411K/F424I
the hydrolytic activities against the PET pentamer is is significantly enhanced as compared with wild-type enzyme
R411K/F424V
the variant shows 10.5times increased MHETase activity in comparison with wild-type enzyme
R411K/F424V
the hydrolytic activities against the PET pentamer is is significantly enhanced as compared with wild-type enzyme
R411K/S416A/F424I
the variant shows 15.3times increased MHETase activity in comparison with wild-type enzyme
R411K/S416A/F424I
the hydrolytic activities against the PET pentamer is is significantly enhanced as compared with wild-type enzyme
R411K/S416A/F424I
the variant shows a higher activity with bis(2-hydroxyethyl) terephthalate and exhibits an enhanced degradation activity against the PET film
S131A
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to less than 5% compared to wild-type value
W130A
mutation results in more space on the binding center and higher activity than the wild-type enzyme
W130A
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 15% compared to wild-type value
W130H
mutation results in more space on the binding center and higher activity than the wild-type enzyme
W130H
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 10% compared to wild-type value
W156A
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 10% compared to wild-type value
Y58A
mutation results in more space on the binding center and higher activity than the wild-type enzyme
Y58A
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 80% compared towild-type value
S131A
Piscinibacter sakaiensis 201-F6
-
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to less than 5% compared to wild-type value
-
additional information
A0A1F4JXW8
molecular dynamics and well-tempered metadynamics simulations are employed to explore the structural basis of the improved catalytic activity of BurPL upon incorporation of the IsPETase-based S214/I218 double substitution. These substitutions increase the flexibility of both active site loop regions harboring key catalytic residues, and the conformational plasticity of the conserved tryptophan within the W-loop
additional information
substitution of the loop connecting beta8-alpha6 with a shorter one from a highly efficient PET-degrading cutinase LCC. This loop exchange, followed by restitution of an active site disulfide bond lost in the process, results in an increase of the optimal activity temperature from 25°C to 45°C, accompanied by a remarkable fivefold enhancement in catalytic activity against amorphous PET films at 45x01C compared with the activity at 25°C. The increase in activity is due to changes in local flexibility in the extended loop and in neighboring active site regions
additional information
engineered thermostable variants of Ideonella sakaiensis PET hydrolase enzyme (IsPETase) are developed using two scaffolding strategies. The first employs SpyCatcher-SpyTag technology to covalently cyclize IsPETase, resulting in increased thermostability that is concomitant with reduced turnover of PET substrates compared to native IsPETase. The second approach using a GFP-nanobody fusion protein (vGFP) as a scaffold yields a construct with a melting temperature of 80°C. This is further increased to 85°C when a thermostable PETase variant (FAST PETase) is scaffolded into vGFP. Thermostability enhancement using the vGFP scaffold does not compromise activity on PET compared to IsPETase
additional information
dual fluorescence-based high-throughput screening (HTS) assay for a representative IsPETase. The two-round HTS of a pilot library consisting of 2850 IsPETase variants yields mutant IsPETases with 1.3-4.9 folds improved activities. Compared to the currently used structure- or computational redesign-based PETase engineering, this HTS approach provides a new strategy for discovery of new beneficial mutation patterns of PETases
additional information
Piscinibacter sakaiensis 201-F6
-
engineered thermostable variants of Ideonella sakaiensis PET hydrolase enzyme (IsPETase) are developed using two scaffolding strategies. The first employs SpyCatcher-SpyTag technology to covalently cyclize IsPETase, resulting in increased thermostability that is concomitant with reduced turnover of PET substrates compared to native IsPETase. The second approach using a GFP-nanobody fusion protein (vGFP) as a scaffold yields a construct with a melting temperature of 80°C. This is further increased to 85°C when a thermostable PETase variant (FAST PETase) is scaffolded into vGFP. Thermostability enhancement using the vGFP scaffold does not compromise activity on PET compared to IsPETase
-
additional information
molecular dynamics and well-tempered metadynamics simulations are employed to explore the structural basis of the improved catalytic activity of Tf Cut upon incorporation of the IsPETase-based S214/I218 double substitution. These substitutions increase the flexibility of both active site loop regions harboring key catalytic residues, and the conformational plasticity of the conserved tryptophan within the W-loop
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
2 h, pH 8.0, about 15% loss of activity in presence of 10 mM CaCl2, about 30% loss of activity without CaCl2
50
56.5
A0A1F4JXW8
melting temperature, wild-type enzyme
60
67.25
69.51
71.3
A0A1F4JXW8
melting ttemperature, mutant enzyme N364C/D418C
80
A0A2H5Z9R5
2 h, pH 8.0, no loss of activity in presence of 10 mM CaCl2, about 20% loss of activity without CaCl2
83.21
Tm-value, mutant enzyme N109A/V129T/A155R/L180C/R198K/A202C/R242C/S291C/G196T
88.3
90
91.6
E5BBQ3
melting temperature, mutant D174C/E253C, presence of 10 mM Ca2+
additional information
90
A0A2H5Z9R5
2 h, pH 8.0, about 20% loss of activity in presence of 10 mM CaCl2
90
G9BY57, C3RYL0
the enzyme (PET2) retains 80% of its relative activity at 90°C after incubation for more than 5 h
additional information
Ca2+ improves enzyme activity and thermal stability, overview
additional information
E5BBQ3
the addition of 10 mM Ca2+ or Mg2+ cations to the enzyme results in an increase of the melting point of about 10°C
additional information
the addition of 10 mM Ca2+ or Mg2+ cations to the enzyme results in an increase of the melting point of about 10°C
additional information
-
the addition of 10 mM Ca2+ or Mg2+ cations to the enzyme results in an increase of the melting point of about 10°C
additional information
E5BBQ3
the addition of 10 mM Ca2+ or Mg2+ cations to the enzyme results in an increase of the melting point of up to 14 degrees
additional information
the addition of 10 mM Ca2+ or Mg2+ cations to the enzyme results in an increase of the melting point of up to 14 degrees
additional information
-
the addition of 10 mM Ca2+ or Mg2+ cations to the enzyme results in an increase of the melting point of up to 14 degrees
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10 mM Ca2+ increases thermal stability
Multigene fusion strategy is introduced for constructing a hydrophobic cell surface display (HCSD) system in Escherichia coli as a robust, recyclable, and sustainable whole-cell catalyst. The HCSD degradation system has excellent stability, maintaining 73% of its initial activity after 7 days of incubation at 40°C and retaining 70% activity after seven cycles
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified to homogeneity using a combined His-tag affinity and ion exchange chromatography approach
recombinant C-terminally His-tagged wild-type enzyme and mutants from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a photosynthetic restoration strategy is used to generate a marker-free transformant line of the green microalga Chlamydomonas reinhardtii in which the PETase from Ideonella sakaiensis is constitutively expressed in the chloroplast
-
cloned into a pET24b vector and transformed into Escherichia coli BL21-Gold(DE3)
expressed in Pichia pastoris. No significant differences between the expression of native Thc_Cut1 and of two glycosylation site knock out mutants (Thc_Cut1_koAsn and Thc_Cut1_koST) concerning the total extracellular protein concentration and volumetric activity are observed
expression in Escherichia coli
expression in Escherichia coli BL21 and in in Bacillus subtilis 168
expression in Escherichia coli BL21(DE3)
expression in Escherichia coli. Expression of IsPETaseMut (a highly active mutant of IsPETase) is systematically explored in Escherichia coli by adopting a series of strategies
-
recombinant expression of C-terminally His-tagged wild-type enzyme and mutants in Escherichia coli strain BL21(DE3)
the crystal structures of PETase in complex with substrate and product analogs provide critical information for understanding the mechanism of action of PETase. The wobbling conformation of W156 is closely related to the binding of substrate and product
the PETase from Ideonella sakaiensis without the N-terminal 29 amino acids is chemically synthesized, ligated into the pET32a vector, and expressed in Escherichia coli
expression in Escherichia coli
A0A1F4JXW8
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
degradation
environmental protection
industry
-
without any enzyme engineering, MG8 already exhibits robust activity across a range of temperature and salinity conditions
analysis
E5BBQ3
determination of enzymatic hydrolysis by measuring the change of intensity of transmitted light due to the scattering effect of PET nanoparticles immobilized in an agarose gel
analysis
E5BBQ3
fluorimetric assay for the fast determination of the activity of polyester-hydrolyzing enzymes in a large number of samples. The assay is robust at different buffer concentrations, reaction times, pH values, and in the presence of proteins and can be used to quantify the amount of terephthalate obtained as the final degradation product of the enzymatic hydrolysis of PET in a microplate format
analysis
-
determination of enzymatic hydrolysis by measuring the change of intensity of transmitted light due to the scattering effect of PET nanoparticles immobilized in an agarose gel
-
analysis
-
fluorimetric assay for the fast determination of the activity of polyester-hydrolyzing enzymes in a large number of samples. The assay is robust at different buffer concentrations, reaction times, pH values, and in the presence of proteins and can be used to quantify the amount of terephthalate obtained as the final degradation product of the enzymatic hydrolysis of PET in a microplate format
-
degradation
a dual enzyme system consisting of the polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 can be employed for the hydrolysis of PET films at 60°C, resulting in an increased amount of soluble products with a lower proportion of mono-(2-hydroxyethyl)terephthalate in the presence of the immobilized TfCa. The dual enzyme system with LC-cutinase produces a 2.4fold higher amount of degradation products compared to Thermobifida fusca enzyme Cut2 after a reaction time of 24 h
degradation
E5BBQ3
mutant D204C/E253C/D174R causes a weight loss of PET films of 25.0% at 70°C after a reaction time of 48 h, compared to 0.3% for wild-type
degradation
E5BBQ3
biodegradability of PET is mainly influenced by the mobility of the polyester chains, which determine the affinity and accessibility of the ester bonds to the enzyme. The hydrolysis rates of enzymatic PET degradation are predominantly controlled by the efficient substrate adsorption rather than by the hydrolysis of the ester bonds. Nanoparticles prepared from PET samples of different crystallinity show a high proportion of amorphous domains and thus in the corresponding biodegradability
degradation
enzyme shows good activity against commercial bottle-derived PET, which is highly crystallized and is was considerably active against PET film at low temperatures
degradation
at 50°C, a maximum hydrolysis rate for poly(ethylene terephthalate) nanoparticles of 0.0033 per min is determined with 80 microg/ml of Tcur_1278. With 50 microg/ml of Tcur_1278, the hydrolysis rate increases 1.8fold at 55°C and 2.6fold at 60°C
degradation
at 50°C, a maximum hydrolysis rate of poly(ethylene terephthalate) nanoparticles of 0.0059 per min is determined with 20 microg/ml of Tcur_0390
degradation
E5BBQ3
exchange of amino acid residues of TfCut2 involved in substrate binding with those present in LC-cutinase, UniProt ID G9BY57, from an uncultured bacterium, leads to enzyme variants with increased PET hydrolytic activity at 65°C. Variant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme
degradation
E5BBQ3, E5BBQ2
the thermostability of the polyester hydrolase is sufficient to degrade semi-crystalline PET films at 65°C in the presence of 10 mM Ca2+ and 10 mM Mg2+ resulting in weight losses of up to 12.9% after a reaction time of 48 h
degradation
due to its low structural stability and solubility, it is difficult to apply standard laboratory-level Ideonella sakaiensis PETase expression and purification procedures in industry. To overcome this difficulty, the expression of IsPETase can be improved by using a secretion system. The extracellular enzyme is successfully produced using pET22b-SPMalE:IsPETase and pET22b-SPLamB:IsPETase expression systems. The secreted IsPETase has PET-degradation activity. The work will be used for development of a new Escherichia coli strain capable of degrading and assimilating PET in its culture medium
degradation
the enzyme can offer an important contribution towards a future sustainable closed loop plastic recycling industry
degradation
enzymatic degradation of poly(ethylene terephthalate) (PET) is promising because this process is safer than conventional industrial approaches. Acceleration of enzymatic degradation of poly(ethylene terephthalate) is reached by surface coating with anionic surfactants
degradation
Tat-independent secretion of polyethylene terephthalate hydrolase PETase in Bacillus subtilis 168 mediated by its native signal peptide. Widespread utilization of polyethylene terephthalate (PET) has caused critical environmental pollution. The enzymatic degradation of PET is a promising solution to this problem. PETase, which exhibits much higher PET hydrolytic activity than other enzymes, is successfully secreted into extracellular milieu from Bacillus subtilis 168 under the direction of its native signal peptide (named SPPETase)
degradation
-
the enzyme is a potential tool to solve the issue of polyester plastic pollution
degradation
E5BBQ3
a dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films. Since the enzymatic PET hydrolysis is inhibited by the degradation intermediate 4-[(2-hydroxyethoxy)carbonyl]benzoate, a dual enzyme system consisting of a polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 is employed for the hydrolysis of PET films at 60°C. HPLC analysis of the reaction products obtained after 24 h of hydrolysis shows an increased amount of soluble products with a lower proportion of 4-[(2-hydroxyethoxy)carbonyl]benzoate in the presence of the immobilized carboxylesterase TfCa. The results indicate a continuous hydrolysis of the inhibitory 4-[(2-hydroxyethoxy)carbonyl]benzoate by the immobilized carboxylesterase TfCa and demonstrate its advantage as a second biocatalyst in combination with a polyester hydrolase for an efficient degradation oft PET films
degradation
-
degradation and bio-functionalization of PET. 2,3-diaminopropionic acid (DAP) is genetically encoded in place of the catalytic serine residue of MG8, thereby converting a PET hydrolase into a covalent binder for bio-functionalization of PET. MG8(DAP), in conjunction with a split green fluorescent protein system, can be used to attach protein cargos to PET as well as other polyester plastics
degradation
polyethylene terephthalate (PET) hydrolase enzymes show promise for enzymatic PET degradation and green recycling of single-use PET vessels representing a major source of global pollution
degradation
enzymatic hydrolysis of PET is an enticing path for plastic degradation and recycling
degradation
enzyme-based depolymerization is a viable approach for recycling of poly(ethylene terephthalate) (PET). Inhibition of IsPETase at high enzyme concentration is an obstacle to the industrial use of the enzyme. This impediment can be partially resolved by adding an organic cosolvent (DMSO), or increasing the substrate surface area by cryomilling. Alternatively, enzyme engineering can be employed to enhance enzyme thermostability to reduce or even eliminate concentration-dependent inhibition. Positive outcome of engineering poly(ethylene terephthalate) hydrolases for enhanced thermostability
degradation
polyethylene terephthalate (PET) is the most abundant plastic waste. It can be degraded by PET hydrolases
degradation
A0A2H5Z9R5
promising PETases for plastic waste recycling and bioremediation applications
degradation
great potential in polyethylene terephthalate (PET) waste management due to its efficient degradation of PET under moderate conditions. Low yield and poor accessibility to bulky substrates hamper its further industrial application. Multigene fusion strategy is introduced for constructing a hydrophobic cell surface display (HCSD) system in Escherichia coli as a robust, recyclable, and sustainable whole-cell catalyst. The truncated outer membrane hybrid protein FadL exposed the PETase and hydrophobic protein HFBII on the surface of Escherichia coli with efficient PET accessibility and degradation performance. Escherichia coli containing the HCSD system changes the surface tension of the bacterial solution, resulting in a smaller contact angle of the system on the PET surface, thus giving a better opportunity for PETase to interact with PET. Pretreatment of PET with HCSD shows rougher surfaces with greater hydrophilicity than the non-pretreated ones. The HCSD system shows excellent sustainable degradation performance for PET bottles with a higher degradation rate than free PETase. The HCSD degradation system has excellent stability, maintaining 73% of its initial activity after 7 days of incubation at 40°C and retaining 70% activity after seven cycles. The HCSD system could be used as a catalyst for efficiently accelerating PET biodegradation
degradation
A0A1F4JXW8
biodegradation of poly(ethylene terephthalate) (PET)
degradation
-
industrially important class of enzymes that catalyze the enzymatic degradation of polyethylene terephatalate (PET), one of the most abundant plastics in the world. The PETase enzyme synthesised in the chloroplast of the microalga Chlamydomonas reinhardtii is active against post-consumer plastics
degradation
enzymatic degradation of poly(ethylene terephthalate) (PET)
degradation
-
degradation and recycling polyethylene terephthalate (PET)
degradation
-
promising biocatalyst for post-consumer poly(ethylene terephthalate) hydrolysis
degradation
-
enzymatic degradation of poly(ethylene terephthalate) (PET)
degradation
degradation and recycling polyethylene terephthalate (PET)
degradation
enzymatic degradation of poly(ethylene terephthalate) (PET)
degradation
enzymatic degradation of poly(ethylene terephthalate) (PET)
degradation
enzymatic degradation of poly(ethylene terephthalate)
degradation
-
mutant D204C/E253C/D174R causes a weight loss of PET films of 25.0% at 70°C after a reaction time of 48 h, compared to 0.3% for wild-type
-
degradation
-
biodegradability of PET is mainly influenced by the mobility of the polyester chains, which determine the affinity and accessibility of the ester bonds to the enzyme. The hydrolysis rates of enzymatic PET degradation are predominantly controlled by the efficient substrate adsorption rather than by the hydrolysis of the ester bonds. Nanoparticles prepared from PET samples of different crystallinity show a high proportion of amorphous domains and thus in the corresponding biodegradability
-
degradation
-
exchange of amino acid residues of TfCut2 involved in substrate binding with those present in LC-cutinase, UniProt ID G9BY57, from an uncultured bacterium, leads to enzyme variants with increased PET hydrolytic activity at 65°C. Variant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme
-
degradation
-
the thermostability of the polyester hydrolase is sufficient to degrade semi-crystalline PET films at 65°C in the presence of 10 mM Ca2+ and 10 mM Mg2+ resulting in weight losses of up to 12.9% after a reaction time of 48 h
-
degradation
-
a dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films. Since the enzymatic PET hydrolysis is inhibited by the degradation intermediate 4-[(2-hydroxyethoxy)carbonyl]benzoate, a dual enzyme system consisting of a polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 is employed for the hydrolysis of PET films at 60°C. HPLC analysis of the reaction products obtained after 24 h of hydrolysis shows an increased amount of soluble products with a lower proportion of 4-[(2-hydroxyethoxy)carbonyl]benzoate in the presence of the immobilized carboxylesterase TfCa. The results indicate a continuous hydrolysis of the inhibitory 4-[(2-hydroxyethoxy)carbonyl]benzoate by the immobilized carboxylesterase TfCa and demonstrate its advantage as a second biocatalyst in combination with a polyester hydrolase for an efficient degradation oft PET films
-
degradation
-
enzymatic degradation of poly(ethylene terephthalate) (PET)
-
degradation
-
at 50°C, a maximum hydrolysis rate for poly(ethylene terephthalate) nanoparticles of 0.0033 per min is determined with 80 microg/ml of Tcur_1278. With 50 microg/ml of Tcur_1278, the hydrolysis rate increases 1.8fold at 55°C and 2.6fold at 60°C
-
degradation
-
at 50°C, a maximum hydrolysis rate of poly(ethylene terephthalate) nanoparticles of 0.0059 per min is determined with 20 microg/ml of Tcur_0390
-
degradation
Piscinibacter sakaiensis 201-F6
-
enzyme shows good activity against commercial bottle-derived PET, which is highly crystallized and is was considerably active against PET film at low temperatures
-
degradation
Piscinibacter sakaiensis 201-F6
-
due to its low structural stability and solubility, it is difficult to apply standard laboratory-level Ideonella sakaiensis PETase expression and purification procedures in industry. To overcome this difficulty, the expression of IsPETase can be improved by using a secretion system. The extracellular enzyme is successfully produced using pET22b-SPMalE:IsPETase and pET22b-SPLamB:IsPETase expression systems. The secreted IsPETase has PET-degradation activity. The work will be used for development of a new Escherichia coli strain capable of degrading and assimilating PET in its culture medium
-
degradation
Piscinibacter sakaiensis 201-F6
-
the enzyme can offer an important contribution towards a future sustainable closed loop plastic recycling industry
-
degradation
Piscinibacter sakaiensis 201-F6
-
enzymatic degradation of poly(ethylene terephthalate) (PET) is promising because this process is safer than conventional industrial approaches. Acceleration of enzymatic degradation of poly(ethylene terephthalate) is reached by surface coating with anionic surfactants
-
degradation
Piscinibacter sakaiensis 201-F6
-
Tat-independent secretion of polyethylene terephthalate hydrolase PETase in Bacillus subtilis 168 mediated by its native signal peptide. Widespread utilization of polyethylene terephthalate (PET) has caused critical environmental pollution. The enzymatic degradation of PET is a promising solution to this problem. PETase, which exhibits much higher PET hydrolytic activity than other enzymes, is successfully secreted into extracellular milieu from Bacillus subtilis 168 under the direction of its native signal peptide (named SPPETase)
-
degradation
Piscinibacter sakaiensis 201-F6
-
polyethylene terephthalate (PET) hydrolase enzymes show promise for enzymatic PET degradation and green recycling of single-use PET vessels representing a major source of global pollution
-
degradation
Piscinibacter sakaiensis 201-F6
-
enzymatic hydrolysis of PET is an enticing path for plastic degradation and recycling
-
degradation
Piscinibacter sakaiensis 201-F6
-
enzyme-based depolymerization is a viable approach for recycling of poly(ethylene terephthalate) (PET). Inhibition of IsPETase at high enzyme concentration is an obstacle to the industrial use of the enzyme. This impediment can be partially resolved by adding an organic cosolvent (DMSO), or increasing the substrate surface area by cryomilling. Alternatively, enzyme engineering can be employed to enhance enzyme thermostability to reduce or even eliminate concentration-dependent inhibition. Positive outcome of engineering poly(ethylene terephthalate) hydrolases for enhanced thermostability
-
degradation
Piscinibacter sakaiensis 201-F6
-
polyethylene terephthalate (PET) is the most abundant plastic waste. It can be degraded by PET hydrolases
-
degradation
Piscinibacter sakaiensis 201-F6
-
great potential in polyethylene terephthalate (PET) waste management due to its efficient degradation of PET under moderate conditions. Low yield and poor accessibility to bulky substrates hamper its further industrial application. Multigene fusion strategy is introduced for constructing a hydrophobic cell surface display (HCSD) system in Escherichia coli as a robust, recyclable, and sustainable whole-cell catalyst. The truncated outer membrane hybrid protein FadL exposed the PETase and hydrophobic protein HFBII on the surface of Escherichia coli with efficient PET accessibility and degradation performance. Escherichia coli containing the HCSD system changes the surface tension of the bacterial solution, resulting in a smaller contact angle of the system on the PET surface, thus giving a better opportunity for PETase to interact with PET. Pretreatment of PET with HCSD shows rougher surfaces with greater hydrophilicity than the non-pretreated ones. The HCSD system shows excellent sustainable degradation performance for PET bottles with a higher degradation rate than free PETase. The HCSD degradation system has excellent stability, maintaining 73% of its initial activity after 7 days of incubation at 40°C and retaining 70% activity after seven cycles. The HCSD system could be used as a catalyst for efficiently accelerating PET biodegradation
-
degradation
Piscinibacter sakaiensis 201-F6
-
enzymatic degradation of poly(ethylene terephthalate) (PET)
-
degradation
Piscinibacter sakaiensis 201-F6
-
degradation and recycling polyethylene terephthalate (PET)
-
degradation
-
industrially important class of enzymes that catalyze the enzymatic degradation of polyethylene terephatalate (PET), one of the most abundant plastics in the world. The PETase enzyme synthesised in the chloroplast of the microalga Chlamydomonas reinhardtii is active against post-consumer plastics
-
environmental protection
the enzyme can offer an important contribution towards a future sustainable closed loop plastic recycling industry
environmental protection
Tat-independent secretion of polyethylene terephthalate hydrolase PETase in Bacillus subtilis 168 mediated by its native signal peptide. Widespread utilization of polyethylene terephthalate (PET) has caused critical environmental pollution. The enzymatic degradation of PET is a promising solution to this problem. PETase, which exhibits much higher PET hydrolytic activity than other enzymes, is successfully secreted into extracellular milieu from Bacillus subtilis 168 under the direction of its native signal peptide (named SPPETase)
environmental protection
-
the enzyme is a potential tool to solve the issue of polyester plastic pollution
environmental protection
the investigation of structure/function relationships can be used to guide further protein engineering to more effectively depolymerize PET and other synthetic polymers, thus informing a biotechnological strategy to help remediate the environmental scourge of plastic accumulation in nature
environmental protection
E5BBQ3
a dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films. Since the enzymatic PET hydrolysis is inhibited by the degradation intermediate 4-[(2-hydroxyethoxy)carbonyl]benzoate, a dual enzyme system consisting of a polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 is employed for the hydrolysis of PET films at 60°C. HPLC analysis of the reaction products obtained after 24 h of hydrolysis shows an increased amount of soluble products with a lower proportion of 4-[(2-hydroxyethoxy)carbonyl]benzoate in the presence of the immobilized carboxylesterase TfCa. The results indicate a continuous hydrolysis of the inhibitory 4-[(2-hydroxyethoxy)carbonyl]benzoate by the immobilized carboxylesterase TfCa and demonstrate its advantage as a second biocatalyst in combination with a polyester hydrolase for an efficient degradation oft PET films
environmental protection
-
a dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films. Since the enzymatic PET hydrolysis is inhibited by the degradation intermediate 4-[(2-hydroxyethoxy)carbonyl]benzoate, a dual enzyme system consisting of a polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 is employed for the hydrolysis of PET films at 60°C. HPLC analysis of the reaction products obtained after 24 h of hydrolysis shows an increased amount of soluble products with a lower proportion of 4-[(2-hydroxyethoxy)carbonyl]benzoate in the presence of the immobilized carboxylesterase TfCa. The results indicate a continuous hydrolysis of the inhibitory 4-[(2-hydroxyethoxy)carbonyl]benzoate by the immobilized carboxylesterase TfCa and demonstrate its advantage as a second biocatalyst in combination with a polyester hydrolase for an efficient degradation oft PET films
-
environmental protection
Piscinibacter sakaiensis 201-F6
-
the enzyme can offer an important contribution towards a future sustainable closed loop plastic recycling industry
-
environmental protection
Piscinibacter sakaiensis 201-F6
-
Tat-independent secretion of polyethylene terephthalate hydrolase PETase in Bacillus subtilis 168 mediated by its native signal peptide. Widespread utilization of polyethylene terephthalate (PET) has caused critical environmental pollution. The enzymatic degradation of PET is a promising solution to this problem. PETase, which exhibits much higher PET hydrolytic activity than other enzymes, is successfully secreted into extracellular milieu from Bacillus subtilis 168 under the direction of its native signal peptide (named SPPETase)
-
environmental protection
Piscinibacter sakaiensis 201-F6
-
the investigation of structure/function relationships can be used to guide further protein engineering to more effectively depolymerize PET and other synthetic polymers, thus informing a biotechnological strategy to help remediate the environmental scourge of plastic accumulation in nature
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wei, R.; Oeser, T.; Then, J.; Kühn, N.; Barth, M.; Schmidt, J.; Zimmermann, W.
Functional characterization and structural modeling of synthetic polyester-degrading hydrolases from Thermomonospora curvata
AMB Express
4
1-10
2014
Thermomonospora curvata (D1A9G5), Thermomonospora curvata (D1A2H1), Thermomonospora curvata DSM 43183 (D1A9G5), Thermomonospora curvata DSM 43183 (D1A2H1)
brenda
Roth, C.; Wei, R.; Oeser, T.; Then, J.; Foellner, C.; Zimmermann, W.; Straeter, N.
Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca
Appl. Microbiol. Biotechnol.
98
7815-7823
2014
Thermobifida fusca (E5BBQ3), Thermobifida fusca
brenda
Barth, M.; Oeser, T.; Wei, R.; Then, J.; Schmidt, J.; Zimmermann, W.
Effect of hydrolysis products on the enzymatic degradation of polyethylene terephthalate nanoparticles by a polyester hydrolase from Thermobifida fusca
Biochem. Eng. J.
93
222-228
2015
Thermobifida fusca (E5BBQ3)
-
brenda
Wei, R.; Oeser, T.; Schmidt, J.; Meier, R.; Barth, M.; Then, J.; Zimmermann, W.
Engineered bacterial polyester hydrolases efficiently degrade polyethylene terephthalate due to relieved product inhibition
Biotechnol. Bioeng.
113
1658-1665
2016
Thermobifida fusca (E5BBQ3), Thermobifida fusca KW3 (E5BBQ3), Thermobifida fusca KW3
brenda
Then, J.; Wei, R.; Oeser, T.; Barth, M.; Belisario-Ferrari, M.R.; Schmidt, J.; Zimmermann, W.
Ca2+ and Mg2+ binding site engineering increases the degradation of polyethylene terephthalate films by polyester hydrolases from Thermobifida fusca
Biotechnol. J.
10
592-598
2015
Thermobifida fusca (E5BBQ3), Thermobifida fusca (E5BBQ2), Thermobifida fusca, Thermobifida fusca KW3 (E5BBQ3), Thermobifida fusca KW3 (E5BBQ2)
brenda
Nimchua, T.; Punnapayak, H.; Zimmermann, W.
Comparison of the hydrolysis of polyethylene terephthalate fibers by a hydrolase from Fusarium oxysporum LCH I and Fusarium solani f. sp. pisi
Biotechnol. J.
2
361-364
2007
Fusarium oxysporum, Fusarium vanettenii, Fusarium oxysporum LCH I, Fusarium vanettenii DSM 62420
brenda
Wei, R.; Oeser, T.; Billig, S.; Zimmermann, W.
A high-throughput assay for enzymatic polyester hydrolysis activity by fluorimetric detection
Biotechnol. J.
7
1517-1521
2012
Thermobifida fusca (E5BBQ3), Thermobifida fusca KW3 (E5BBQ3)
brenda
Then, J.; Wei, R.; Oeser, T.; Gerdts, A.; Schmidt, J.; Barth, M.; Zimmermann, W.
A disulfide bridge in the calcium binding site of a polyester hydrolase increases its thermal stability and activity against polyethylene terephthalate
FEBS open bio
6
425-432
2016
Thermobifida fusca (E5BBQ3), Thermobifida fusca KW3 (E5BBQ3)
brenda
Schmidt, J.; Wei, R.; Oeser, T.; Belisario-Ferrari, M.R.; Barth, M.; Then, J.; Zimmermann, W.
Effect of Tris, MOPS, and phosphate buffers on the hydrolysis of polyethylene terephthalate films by polyester hydrolases
FEBS open bio
6
919-927
2016
Thermobifida fusca (E5BBQ3), Thermobifida fusca KW3 (E5BBQ3), Thermobifida fusca KW3, uncultured bacterium (G9BY57)
brenda
Wei, R.; Oeser, T.; Barth, M.; Weigl, N.; Lübs, A.; Schulz-Siegmund, M.; Hacker, M.; Zimmermann, W.
Turbidimetric analysis of the enzymatic hydrolysis of polyethylene terephthalate nanoparticles
J. Mol. Catal. B
103
72-78
2014
Thermobifida fusca (E5BBQ3), Thermobifida fusca KW3 (E5BBQ3)
-
brenda
Yoshida, S.; Hiraga, K.; Takehana, T.; Taniguchi, I.; Yamaji, H.; Maeda, Y.; Toyohara, K.; Miyamoto, K.; Kimura, Y.; Oda, K.
A bacterium that degrades and assimilates poly(ethylene terephthalate)
Science
351
1196-1199
2016
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Danso, D.; Schmeisser, C.; Chow, J.; Zimmermann, W.; Wei, R.; Leggewie, C.; Li, X.; Hazen, T.; Streit, W.R.
New insights into the function and global distribution of polyethylene terephthalate (PET)-degrading bacteria and enzymes in marine and terrestrial metagenomes
Appl. Environ. Microbiol.
84
e02773-17
2018
Piscinibacter sakaiensis (A0A0K8P6T7), Saccharomonospora viridis (W0TJ64), Thermobifida alba (E9LVH7), Thermobifida cellulosilytica (E9LVH9), Thermobifida fusca (E5BBQ3), Thermobifida fusca (E9LVI0), Thermobifida halotolerans (H6WX58), Thermomonospora curvata (D1A9G5), Thermomonospora curvata DSM 43183 (D1A9G5), uncultured bacterium (G9BY57), uncultured bacterium (C3RYL0)
brenda
Seo, H.; Kim, S.; Son, H.F.; Sagong, H.Y.; Joo, S.; Kim, K.J.
Production of extracellular PETase from Ideonella sakaiensis using sec-dependent signal peptides in E. coli
Biochem. Biophys. Res. Commun.
508
250-255
2018
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Fecker, T.; Galaz-Davison, P.; Engelberger, F.; Narui, Y.; Sotomayor, M.; Parra, L.P.; Ramirez-Sarmiento, C.A.
Active site flexibility as a hallmark for efficient PET degradation by I. sakaiensis PETase
Biophys. J.
114
1302-1312
2018
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Barth, M.; Honak, A.; Oeser, T.; Wei, R.; Belisario-Ferrari, M.R.; Then, J.; Schmidt, J.; Zimmermann, W.
A dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films
Biotechnol. J.
11
1082-1087
2016
uncultured bacterium (G9BY57), Thermobifida fusca (E5BBQ3), Thermobifida fusca KW3 (E5BBQ3), Thermobifida fusca KW3
brenda
Liu, B.; He, L.; Wang, L.; Li, T.; Li, C.; Liu, H.; Luo, Y.; Bao, R.
Protein crystallography and site-direct mutagenesis analysis of the poly(ethylene terephthalate) hydrolase PETase from Ideonella sakaiensis
ChemBioChem
19
1471-1475
2018
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Furukawa, M.; Kawakami, N.; Oda, K.; Miyamoto, K.
Acceleration of enzymatic degradation of poly(ethylene terephthalate) by surface coating with anionic surfactants
ChemSusChem
11
4018-4025
2018
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Ma, Y.; Yao, M.; Li, B.; Ding, M.; He, B.; Chen, S.; Zhou, X.; Yuan, Y.
Enhanced poly(ethylene terephthalate) hydrolase activity by protein engineering
Engineering
4
888-893
2018
Piscinibacter sakaiensis
-
brenda
Chen, C.C.; Han, X.; Ko, T.P.; Liu, W.; Guo, R.T.
Structural studies reveal the molecular mechanism of PETase
FEBS J.
285
3717-3723
2018
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Gamerith, C.; Vastano, M.; Ghorbanpour, S.M.; Zitzenbacher, S.; Ribitsch, D.; Zumstein, M.T.; Sander, M.; Herrero Acero, E.; Pellis, A.; Guebitz, G.M.
Enzymatic degradation of aromatic and aliphatic polyesters by P. pastoris expressed cutinase 1 from Thermobifida cellulosilytica
Front. Microbiol.
8
938
2017
Thermobifida cellulosilytica (E9LVH8)
brenda
Huang, X.; Cao, L.; Qin, Z.; Li, S.; Kong, W.; Liu, Y.
Tat-independent secretion of polyethylene terephthalate hydrolase PETase in Bacillus subtilis 168 mediated by its native signal peptide
J. Agric. Food Chem.
66
13217-13227
2018
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
de Castro, A.M.; Carniel, A.; Nicomedes Junior, J.; da Conceicao Gomes, A.; Valoni, E.
Screening of commercial enzymes for poly(ethylene terephthalate) (PET) hydrolysis and synergy studies on different substrate sources
J. Ind. Microbiol. Biotechnol.
44
835-844
2017
Aspergillus oryzae, Burkholderia cepacia, Diutina rugosa, Moesziomyces antarcticus, Mycothermus thermophilus, Pseudomonas fluorescens, Rhizomucor miehei, Rhizopus arrhizus, Rhizopus niveus, Sus scrofa, Thermomyces lanuginosus, Triticum aestivum
brenda
Han, X.; Liu, W.; Huang, J.W.; Ma, J.; Zheng, Y.; Ko, T.P.; Xu, L.; Cheng, Y.S.; Chen, C.C.; Guo, R.T.
Structural insight into catalytic mechanism of PET hydrolase
Nat. Commun.
8
2106
2017
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Joo, S.; Cho, I.; Seo, H.; Son, H.; Sagong, H.; Shin, T.; Choi, S.; Lee, S.; Kim, K.
Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation
Nat. Commun.
9
382
2018
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Austin, H.P.; Allen, M.D.; Donohoe, B.S.; Rorrer, N.A.; Kearns, F.L.; Silveira, R.L.; Pollard, B.C.; Dominick, G.; Duman, R.; El Omari, K.; Mykhaylyk, V.; Wagner, A.; Michener, W.E.; Amore, A.; Skaf, M.S.; Crowley, M.F.; Thorne, A.W.; Johnson, C.W.; Woodcock, H.L.; McGeehan, J.E.; Beckham, G.T.
Characterization and engineering of a plastic-degrading aromatic polyesterase
Proc. Natl. Acad. Sci. USA
115
E4350-E4357
2018
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Brackmann, R.; de Oliveira Veloso, C.; de Castro, A.M.; Langone, M.A.P.
Enzymatic post-consumer poly(ethylene terephthalate) (PET) depolymerization using commercial enzymes
3 Biotech
13
135
2023
Mycothermus thermophilus
brenda
Sagong, H.; Seo, H.; Kim, T.; Son, H.; Joo, S.; Lee, S.; Kim, S.; Woo, J.; Hwang, S.; Kim, K.
Decomposition of the PET film by MHETase using exo-PETase function
ACS Catal.
10
4805-4812
2020
Piscinibacter sakaiensis (A0A0K8P8E7), Piscinibacter sakaiensis 201-F6 (A0A0K8P8E7)
-
brenda
Crnjar, A.; Grinen, A.; Kamerlin, S.; Ramírez-Sarmiento, C.
Conformational selection of a tryptophan side chain drives the generalized increase in activity of PET hydrolases through a Ser/Ile double mutation
ACS Org. Inorg. Au
3
109-119
2023
Burkholderiales bacterium RIFCSPLOWO2_02_FULL_57_36 (A0A1F4JXW8), Thermobifida fusca (Q6A0I4), Piscinibacter sakaiensis (A0A0K8P6T7)
brenda
Kawai, F.; Furushima, Y.; Mochizuki, N.; Muraki, N.; Yamashita, M.; Iida, A.; Mamoto, R.; Tosha, T.; Iizuka, R.; Kitajima, S.
Efficient depolymerization of polyethylene terephthalate (PET) and polyethylene furanoate by engineered PET hydrolase Cut190
AMB Express
12
134
2022
Saccharomonospora viridis (W0TJ64), Saccharomonospora viridis AHK190 (W0TJ64)
brenda
Eiamthong, B.; Meesawat, P.; Wongsatit, T.; Jitdee, J.; Sangsri, R.; Patchsung, M.; Aphicho, K.; Suraritdechachai, S.; Huguenin-Dezot, N.; Tang, S.; Suginta, W.; Paosawatyanyong, B.; Babu, M.M.; Chin, J.W.; Pakotiprapha, D.; Bhanthumnavin, W.; Uttamapinant, C.
Discovery and genetic code expansion of a polyethylene terephthalate hydrolase from the human saliva metagenome for the degradation and bio-functionalization of PET
Angew. Chem. Int. Ed. Engl.
61
e202203061
2022
Homo sapiens
brenda
Puspitasari, N.; Tsai, S.L.; Lee, C.K.
Fungal hydrophobin RolA enhanced PETase hydrolysis of polyethylene terephthalate
Appl. Biochem. Biotechnol.
193
1284-1295
2021
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Yin, Q.; You, S.; Zhang, J.; Qi, W.; Su, R.
Enhancement of the polyethylene terephthalate and mono-(2-hydroxyethyl) terephthalate degradation activity of Ideonella sakaiensis PETase by an electrostatic interaction-based strategy
Biores. Technol.
364
128026
2022
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Sana, B.; Ding, K.; Siau, J.W.; Pasula, R.R.; Chee, S.; Kharel, S.; Lena, J.H.; Goh, E.; Rajamani, L.; Lam, Y.M.; Lim, S.; Ghadessy, J.F.
Thermostability enhancement of polyethylene terephthalate degrading PETase using self- and nonself-ligating protein scaffolding approaches
Biotechnol. Bioeng.
120
3200-3209
2023
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Duan, S.; Zhang, N.; Chao, T.; Wu, Y.; Wang, M.
The structural and molecular mechanisms of type II PETases a mini review
Biotechnol. Lett.
45
1249-1263
2023
Burkholderiales bacterium (A0A1F4JXW8), Halopseudomonas aestusnigri (A0A1H6AD45), Piscinibacter gummiphilus (A0A1W6L588), Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Castro-Rodríguez, J.; Rodríguez-Sotres, R.; Farrés, A.
Determinants for an efficient enzymatic catalysis in poly(ethylene terephthalate) degradation
Catalysts
13
591
2023
Mycothermus thermophilus, Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7), Saccharomonospora viridis (W0TJ64), Thermobifida cellulosilytica (E9LVH9), Thermobifida cellulosilytica (E9LVH8), Thermobifida cellulosilytica DSM 44535 (E9LVH8), Thermobifida cellulosilytica DSM 44535 (E9LVH9), Thermobifida fusca (Q6A0I4)
-
brenda
Baath, J.A.; Borch, K.; Jensen, K.; Brask, J.; Westh, P.
Comparative biochemistry of four polyester (PET) hydrolases
ChemBioChem
22
1627-1637
2021
Piscinibacter sakaiensis
brenda
Schubert, S.; Schaller, K.; Baath, J.A.; Hunt, C.; Borch, K.; Jensen, K.; Brask, J.; Westh, P.
Reaction pathways for the enzymatic degradation of poly(ethylene terephthalate) what characterizes an efficient PET-hydrolase?
ChemBioChem
24
e202200516
2023
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Liu, K.; Xu, Z.; Zhao, Z.; Chen, Y.; Chai, Y.; Ma, L.; Li, S.
A dual fluorescence assay enables high-throughput screening for poly(ethylene terephthalate) hydrolases
ChemSusChem
16
e202202019
2023
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Avilan, L.; Lichtenstein, B.R.; Koenig, G.; Zahn, M.; Allen, M.D.; Oliveira, L.; Clark, M.; Bemmer, V.; Graham, R.; Austin, H.P.; Dominick, G.; Johnson, C.W.; Beckham, G.T.; McGeehan, J.E.; Pickford, A.R.
Concentration-dependent inhibition of mesophilic PETases on poly(ethylene terephthalate) can be eliminated by enzyme engineering
ChemSusChem
16
e202202277
2023
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Pasula, R.R.; Lim, S.; Ghadessy, F.J.; Sana, B.
The influences of substrates physical properties on enzymatic PET hydrolysis Implications for PET hydrolase engineering
Eng. Biol.
6
17-22
2022
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Wang, X.; Song, C.; Qi, Q.; Zhang, Y.; Li, R.; Huo, L.
Biochemical characterization of a polyethylene terephthalate hydrolase and design of high-throughput screening for its directed evolution
Eng. Microbiol.
2
100020
2022
Caldimonas brevitalea, Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
-
brenda
Aer, L.; Jiang, Q.; Gul, I.; Qi, Z.; Feng, J.; Tang, L.
Overexpression and kinetic analysis of Ideonella sakaiensis PETase for polyethylene terephthalate (PET) degradation
Environ. Res.
212
113472
2022
Piscinibacter sakaiensis
brenda
Xi, X.; Ni, K.; Hao, H.; Shang, Y.; Zhao, B.; Qian, Z.
Secretory expression in Bacillus subtilis and biochemical characterization of a highly thermostable polyethylene terephthalate hydrolase from bacterium HR29
Enzyme Microb. Technol.
143
109715
2021
bacterium HR29 (A0A2H5Z9R5), Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Gao, R.; Pan, H.; Lian, J.
Recent advances in the discovery, characterization, and engineering of poly(ethylene terephthalate) (PET) hydrolases
Enzyme Microb. Technol.
150
109868
2021
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Liu, Y.; Liu, C.; Liu, H.; Zeng, Q.; Tian, X.; Long, L.; Yang, J.
Catalytic features and thermal adaptation mechanisms of a deep sea bacterial cutinase-type poly(ethylene terephthalate) hydrolase
Front. Bioeng. Biotechnol.
10
865787
2022
Marinactinospora thermotolerans (A0A1T4KK94), Marinactinospora thermotolerans DSM 45154 (A0A1T4KK94), Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Jia, Y.; Samak, N.A.; Hao, X.; Chen, Z.; Wen, Q.; Xing, J.
Hydrophobic cell surface display system of PETase as a sustainable biocatalyst for PET degradation
Front. Microbiol.
13
1005480
2022
Piscinibacter sakaiensis (A0A0K8P6T7), Piscinibacter sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Sagong, H.Y.; Kim, S.; Lee, D.; Hong, H.; Lee, S.H.; Seo, H.; Kim, K.J.
Structural and functional characterization of an auxiliary domain-containing PET hydrolase from Burkholderiales bacterium
J. Hazard. Mater.
429
128267
2022
Burkholderiales bacterium RIFCSPLOWO2_02_FULL_57_36 (A0A1F4JXW8)
brenda
Eugenio, E.; Campisano, I.; de Castro, A.; Coelho, M.; Langone, M.
Kinetic modeling of the post-consumer poly(ethylene terephthalate) hydrolysis catalyzed by cutinase from Humicola insolens
J. Polym. Environ.
30
1627-1637
2022
Mycothermus thermophilus
-
brenda
Huang, D.; Zhang, L.; Sun, Y.
Rational design of disulfide bridges in BbPETaseCD for enhancing the enzymatic performance in PET degradation
Molecules
28
3528
2023
Burkholderiales bacterium RIFCSPLOWO2_02_FULL_57_36 (A0A1F4JXW8)
brenda
Erickson, E.; Gado, J.E.; Avilan, L.; Bratti, F.; Brizendine, R.K.; Cox, P.A.; Gill, R.; Graham, R.; Kim, D.J.; Koenig, G.; Michener, W.E.; Poudel, S.; Ramirez, K.J.; Shakespeare, T.J.; Zahn, M.; Boyd, E.S.; Payne, C.M.; DuBois, J.L.; Pickford, A.R.; Beckham, G.T.; McGeehan, J.E.
Sourcing thermotolerant poly(ethylene terephthalate) hydrolase scaffolds from natural diversity
Nat. Commun.
13
7850
2022
Thermobifida fusca (Q6A0I4), Thermobifida fusca (WP_104613137.1), Thermobifida cellulosilytica, Thermobifida cellulosilytica (E9LVH9), Thermobifida alba (D4Q9N1), Marinactinospora thermotolerans (A0A1T4KK94), Saccharopolyspora flava (A0A1I6PTF4), Micromonosporaceae bacterium (A0A3D5ATI9), Ketobacter sp. (A0A3L8BW54), Nocardioidaceae bacterium Broad-1 (E9UPM2), Caldimonas taiwanensis, Thermobifida cellulosilytica DSM 44535 (E9LVH9), Marinactinospora thermotolerans DSM 45145 (A0A1T4KK94)
brenda
Hong, H.; Ki, D.; Seo, H.; Park, J.; Jang, J.; Kim, K.J.
Discovery and rational engineering of PET hydrolase with both mesophilic and thermophilic PET hydrolase properties
Nat. Commun.
14
4556
2023
Cryptosporangium aurantiacum (A0A1M7II12)
brenda
Blazquez-Sanchez, P.; Vargas, J.A.; Furtado, A.A.; Grinen, A.; Leonardo, D.A.; Sculaccio, S.A.; Pereira, H.D.; Sonnendecker, C.; Zimmermann, W.; Diez, B.; Garratt, R.C.; Ramirez-Sarmiento, C.A.
Engineering the catalytic activity of an Antarctic PET-degrading enzyme by loop exchange
Protein Sci.
32
e4757
2023
Moraxella sp. TA144 (P19833)
brenda
Di Rocco, G.; Taunt, H.N.; Berto, M.; Jackson, H.O.; Piccinini, D.; Carletti, A.; Scurani, G.; Braidi, N.; Purton, S.
A PETase enzyme synthesised in the chloroplast of the microalga Chlamydomonas reinhardtii is active against post-consumer plastics
Sci. Rep.
13
10028
2023
Piscinibacter sakaiensis, Piscinibacter sakaiensis TN72
brenda
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