idesa-peth

Ideonella sakaiensis (strain 201-F6) (Piscinibacter sakaiensis)Poly(ethylene terephthalate) hydrolase (plastic degradation), PETase IsPETase ThermoPETase DuraPETase FastPETase HotPETase

Comment

Polyethylene terephthalate is the most common thermoplastic polymer resin of the polyester family and is used in fibers for clothing, containers for liquids and foods. This enzyme hydrolyses PET in bis(2-hydroxyethyl)-TPA (BHET), MHET (Mono(ethylene terephthalate)), and TPA (Terephthalic-acid). (ThermoPETase, with only three mutations with respect to the wild-type homolog (S121E\/D186H\/R280A) Sonet al.2019)\; Cui et al. 2021 computationally redesigned PETase to provide a new variant (DuraPETase) which, after its synthesis, exhibited a high melting temperature (a Tm value of 77 C compared to that reported for PETase, Tm = 46 C) and strikingly enhanced degradation toward semicrystalline PET films at mild temperatures (over 300-fold)\;(HotPETase Bell 2022) Lu et al. 2022 designed the FAST-PETase with five mutations with respect to wild-type PETase (N233K\/R224Q\/S121E\/D186H\/R280A) and exhibits a superior catalytic activity in the 3050 C range compared to wild-type PETase and all other so far proposed mutants. FAST-PETase is able to completely biodegrade untreated and postconsumer PET waste from different products in 1 week. (Turbo PETase (BhrPETaseH218S\/F222I\/A209R\/D238K\/A251C\/A281C\/W104L\/F243T)Cui et al. 2024)

Relationship

Family : Polyesterase-lipase-cutinase

Block : L

Position in NCBI Life Tree : Ideonella sakaiensis

(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)

> cellular organisms N E > Bacteria N E > Proteobacteria N E > Betaproteobacteria N E > Burkholderiales N E > unclassified Burkholderiales N E > Burkholderiales Genera incertae sedis N E > Ideonella N E > Ideonella sakaiensis N E

Molecular evidence

No mutation

5XFY - Crystal structure of a novel PET hydrolase S131A mutant from Ideonella sakaiensis 201-F6 5XFZ - Crystal structure of a novel PET hydrolase R103G\/S131A mutant from Ideonella sakaiensis 201-F6 5XG0 - Crystal structure of a novel PET hydrolase from Ideonella sakaiensis 201-F6 5XH2 - Crystal structure of a novel PET hydrolase R103G\/S131A mutant in complex with pNP from Ideonella sakaiensis 201-F6 5XH3 - Crystal structure of a novel PET hydrolase R103G\/S131A mutant in complex with HEMT from Ideonella sakaiensis 201-F6 5XJH - Crystal strcuture of PETase from Ideonella sakaiensis 5YFE - Enzymatic and structural characterization of the poly (ethylene terephthalate) bacterial hydrolase PETase from Ideonella sakaiensis 5YNS - Crystal strcuture of PETase R280A mutant from Ideonella sakaiensis 6ANE - Active site flexibility as a hallmark for efficient PET degradation by Ideonella sakaiensis PETase 6EQD - Crystal structure of a polyethylene terephthalate degrading hydrolase from Ideonella sakaiensis collected at long wavelength 6EQE - High resolution crystal structure of a polyethylene terephthalate degrading hydrolase from Ideonella sakaiensis 6EQF - Crystal structure of a polyethylene terephthalate degrading hydrolase from Ideonella sakaiensis in spacegroup P212121 6EQG - Crystal structure of a polyethylene terephthalate degrading hydrolase from Ideonella sakaiensis in spacegroup P21 6EQH - Crystal structure of a polyethylene terephthalate degrading hydrolase from Ideonella sakaiensis in spacegroup C2221 6IJ3 - Crystal structure of PETase S121D, D186H mutant from Ideonella sakaiensis 6IJ4 - Crystal structure of PETase S121E, D186H mutant from Ideonella sakaiensis 6IJ5 - Crystal structure of PETase P181A mutant from Ideonella sakaiensis 6IJ6 - Crystal structure of PETase S121E, D186H, R280A mutant from Ideonella sakaiensis 6ILW - Crystal structure of PETase from Ideonella sakaiensis 6ILX - Crystal structure of PETase W159F mutant from Ideonella sakaiensis 6KUO - Crystal strcuture of PETase N246D mutant from Ideonella sakaiensis 6KUQ - Crystal strcuture of PETase A248D, R280K mutant from Ideonella sakaiensis 6KUS - Crystal strcuture of PETase S121E, D186H, S242T, N246D mutant from Ideonella sakaiensis 6KY5 - Crystal strcuture of PETase from Ideonella sakaiensis redesigned for plasticbiodegradation by GRAPE strategy T140D\/W159H\/I168R\/S188Q\/S214H\/L117F\/Q119Y DuraPETase 6QGC - Structure of a plastic degrading enzyme MHETase from Ideonella sakaiensis without ligand 7CQB - Crystal structure of mutant of a Petase mutant 7CY0 - Crystal structure of a new Petase triple mutant 7OSB - Crystal Structure of a Double Mutant PETase (S238F\/W159H) from Ideonella sakaiensis 7QVH - The crystal structure of HotPETase, an evolved thermostable variant of IsPETase 7SH6 - Crystal structure of a PET hydrolase mutant from Ideonella Sakaiensis 7VWN - The structure of an engineered PET hydrolase (variant of IsPETase Ideonella sakaiensis) 7XTW - Structure of Ideonella sakaiensis cutinase IsPETase, MHET-bound IsPETase S160A 8CRU - The crystal structure of GrAnc8, an evolved variant of IsPETase Ideonella sakaiensis Reconstruction 008 8D1D - The crystal structure of PROSS5 PETase, an evolved variant of IsPETase Ideonella sakaiensis 8GU4 - Poly(ethylene terephthalate) hydrolase IsPETase-linker Ideonella sakaiensis 8GU5 - Poly(ethylene terephthalate) hydrolase Wild type IsPETase Ideonella sakaiensis 8H5J - Crystal structure of PETase S121E\/A180V\/P181V\/D186H\/N233C\/S242T\/N246D\/S282C mutant from Ideonella sakaiensis 8H5K - Crystal structure of PETase N37D\/S121E\/R132E\/A171C\/A180V\/P181V\/D186H\/S193C\/R224E\/N233C\/S242T\/N246D\/S282C mutant from Ideonella sakaiensis 8H5L - Crystal structure of PETase N37D\/S121E\/R132E\/A171C\/A180V\/P181V\/D186H\/S193C\/A202C\/V211C\/S214Y\/R224E\/N233C\/S242T\/N246D\/N275C\/S282C\/F284C mutant from Ideonella sakaiensis 8H5M - Crystal structure of PETase S121E\/D186H\/N233C\/S242T\/N246D\/S282C mutant from Ideonella sakaiensis 8H5N - WITHDRAWN Crystal structure of PETase S121E\/A180V\/D186H\/N233C\/S242T\/N246D\/S282C mutant from Ideonella sakaiensis 8H5O - Crystal structure of PETase S121E\/P181V\/D186H\/N233C\/S242T\/N246D\/S282C mutant from Ideonella sakaiensis 8H83 - Crystal structure of a IsPETase variant V22 from Ideonella sakaiensis 8J17 - Structure of Ideonella sakaiensis cutinase IsPETase, thermostable S92P\/D157A variant 8J45 - Crystal structure of a Pichia pastoris-expressed IsPETase variant 8J5N - Crystal structure of a IsPETase variant V20 from Ideonella sakaiensis 8VE9 - Structure of Ideonella sakaiensis cutinase IsPETase - ACCCETN mutant - CombiPETase 8VEK - Structure of Ideonella sakaiensis cutinase IsPETase - ACC mutant 8VEL - Structure of Ideonella sakaiensis cutinase IsPETase - ACCCC mutant 8VEM - Structure of Ideonella sakaiensis cutinase IsPETase - ACCE mutant

No kinetic

No disease

Database

Sequence

Peptide

MNFPRASRLM QAAVLGGLMA VSAAATAQTN PYARGPNPTA ASLEASAGPF TVRSFTVSRP SGYGAGTVYY PTNAGGTVGA IAIVPGYTAR QSSIKWWGPR LASHGFVVIT IDTNSTLDQP SSRSSQQMAA LRQVASLNGT SSSPIYGKVD TARMGVMGWS MGGGGSLISA ANNPSLKAAA PQAPWDSSTN FSSVTVPTLI FACENDSIAP VNSSALPIYD SMSRNAKQFL EINGGSHSCA NSGNSNQALI GKKGVAWMKR FMDNDTRYST FACENPNSTR VSDFRTANCS

References (73)

Title : New Labeled PET Analogues Enable the Functional Screening and Characterization of PET-Degrading Enzymes - Taxeidis_2024_ACS.Sustain.Chem.Eng_12_5943
Author(s) : Taxeidis G , Djapovic M , Nikolaivits E , Maslak V , Nikodinovic-Runic J , Topakas E
Ref : ACS Sustain Chem Eng , 12 :5943 , 2024
Abstract :
PubMedSearch : Taxeidis_2024_ACS.Sustain.Chem.Eng_12_5943
PubMedID: 38903150
Gene_locus related to this paper: idesa-peth , 9bact-g9by57 , morsp-lip1

Title : Exploring the substrate spectrum of phylogenetically distinct bacterial polyesterases - Makryniotis_2024_Biotechnol.J__e2400053
Author(s) : Makryniotis K , Nikolaivits E , Taxeidis G , Nikodinovic-Runic J , Topakas E
Ref : Biotechnol J , :e2400053 , 2024
Abstract :
PubMedSearch : Makryniotis_2024_Biotechnol.J__e2400053
PubMedID: 38593303
Gene_locus related to this paper: idesa-peth , comac-polest , strex-lipas , psefl-phaz

Title : The reaction mechanism of the Ideonella sakaiensis PETase enzyme - Burgin_2024_Commun.Chem_7_65
Author(s) : Burgin T , Pollard BC , Knott BC , Mayes HB , Crowley MF , McGeehan JE , Beckham GT , Woodcock HL
Ref : Commun Chem , 7 :65 , 2024
Abstract :
PubMedSearch : Burgin_2024_Commun.Chem_7_65
PubMedID: 38538850
Gene_locus related to this paper: idesa-peth

Title : Complete decomposition of poly(ethylene terephthalate) by crude PET hydrolytic enzyme produced in Pichia pastoris - Chen_2024_Chem.Eng.J_481_148418
Author(s) : Chen CC , Li X , Min J , Zeng Z , Ning Z , He H , Long X , Niu D , Peng R , Liu X , Yang Y , Huang JW , Guo RT
Ref : Chemical Engineering Journal , 481 :148418 , 2024
Abstract :
PubMedSearch : Chen_2024_Chem.Eng.J_481_148418
PubMedID:
Gene_locus related to this paper: idesa-peth

Title : Efficient Depolymerization of Poly(ethylene 2,5-furanoate) Using Polyester Hydrolases - Kumar_2024_ACS.Sustain.Chem.Eng_12_9658
Author(s) : Kumar V , Pellis A , Wimmer R , Popok V , Christiansen JC , Varrone C
Ref : ACS Sustain Chem Eng , 12 :9658 , 2024
Abstract :
PubMedSearch : Kumar_2024_ACS.Sustain.Chem.Eng_12_9658
PubMedID: 38966237
Gene_locus related to this paper: idesa-peth , 9bact-g9by57

Title : Molecular engineering of PETase for efficient PET biodegradation - Wang_2024_Ecotoxicol.Environ.Saf_280_116540
Author(s) : Wang T , Yang WT , Gong YM , Zhang YK , Fan XX , Wang GC , Lu ZH , Liu F , Liu XH , Zhu YS
Ref : Ecotoxicology & Environmental Safety , 280 :116540 , 2024
Abstract :
PubMedSearch : Wang_2024_Ecotoxicol.Environ.Saf_280_116540
PubMedID: 38833982
Gene_locus related to this paper: idesa-peth

Title : Computation-Based Design of Salt Bridges in PETase for Enhanced Thermostability and Performance for PET Degradation - Qu_2023_Chembiochem_24_e202300373
Author(s) : Qu Z , Chen K , Zhang L , Sun Y
Ref : Chembiochem , 24 :e202300373 , 2023
Abstract :
PubMedSearch : Qu_2023_Chembiochem_24_e202300373
PubMedID: 37639367
Gene_locus related to this paper: idesa-peth

Title : Efficient polyethylene terephthalate biodegradation by an engineered Ideonella sakaiensis PETase with a fixed substrate-binding W156 residue - ?Yin_2023_Green.Chemistry__
Author(s) : Yin Q , Zhang J , Ma S , Gu T , Wang M , You S , Ye S , Su R , Wang Y , Qi W
Ref : Green Chemistry , : , 2023
Abstract :
PubMedSearch : ?Yin_2023_Green.Chemistry__
PubMedID:
Gene_locus related to this paper: idesa-peth

Title : Balance-directed protein engineering of IsPETase enhances both PET hydrolysis activity and thermostability - Lee_2023_bioRxiv__
Author(s) : Lee SH , Seo H , Hong H , Park J , Ki D , Kim M , Kim HJ , Kim KJ
Ref : Biorxiv , : , 2023
Abstract :
PubMedSearch : Lee_2023_bioRxiv__
PubMedID:
Gene_locus related to this paper: idesa-peth

Title : Three-directional engineering of IsPETase with enhanced protein yield, activity, and durability - Lee_2023_J.Hazard.Mater_459_132297
Author(s) : Lee SH , Seo H , Hong H , Park J , Ki D , Kim M , Kim HJ , Kim KJ
Ref : J Hazard Mater , 459 :132297 , 2023
Abstract :
PubMedSearch : Lee_2023_J.Hazard.Mater_459_132297
PubMedID: 37595467
Gene_locus related to this paper: idesa-peth

Title : A PETase enzyme synthesised in the chloroplast of the microalga Chlamydomonas reinhardtii is active against post-consumer plastics - Di Rocco_2023_Sci.Rep_13_10028
Author(s) : Di Rocco G , Taunt HN , Berto M , Jackson HO , Piccinini D , Carletti A , Scurani G , Braidi N , Purton S
Ref : Sci Rep , 13 :10028 , 2023
Abstract :
PubMedSearch : Di Rocco_2023_Sci.Rep_13_10028
PubMedID: 37340047
Gene_locus related to this paper: idesa-peth

Title : Degradation of PET Bottles by an Engineered Ideonella sakaiensis PETase - Sevilla_2023_Polymers.(Basel)_15_1779
Author(s) : Sevilla ME , Garcia MD , Perez-Castillo Y , Armijos-Jaramillo V , Casado S , Vizuete K , Debut A , Cerda-Mejia L
Ref : Polymers (Basel) , 15 :1779 , 2023
Abstract :
PubMedSearch : Sevilla_2023_Polymers.(Basel)_15_1779
PubMedID: 37050393
Gene_locus related to this paper: idesa-peth

Title : Complete bio-degradation of poly(butylene adipate-co-terephthalate) via engineered cutinases - Yang_2023_Nat.Commun_14_1645
Author(s) : Yang Y , Min J , Xue T , Jiang P , Liu X , Peng R , Huang JW , Qu Y , Li X , Ma N , Tsai FC , Dai L , Zhang Q , Liu Y , Chen CC , Guo RT
Ref : Nat Commun , 14 :1645 , 2023
Abstract :
PubMedSearch : Yang_2023_Nat.Commun_14_1645
PubMedID: 36964144
Gene_locus related to this paper: idesa-peth , thefu-q6a0i4

Title : Conformational Selection of a Tryptophan Side Chain Drives the Generalized Increase in Activity of PET Hydrolases through a Ser\/Ile Double Mutation - Crnjar_2023_ACS.Org.Inorg.Au__
Author(s) : Crnjar A , Grinen A , Kamerlin SCL , Ramirez-Sarmiento CA
Ref : ACS Organic & Inorganic Au , : , 2023
Abstract :
PubMedSearch : Crnjar_2023_ACS.Org.Inorg.Au__
PubMedID:
Gene_locus related to this paper: 9burk-a0a1f4jxw8 , idesa-peth , 9bact-g9by57 , thefu-q6a0i4

Title : Insights into the Enhancement of the Poly(ethylene terephthalate) Degradation by FAST-PETase from Computational Modeling - Garcia-Meseguer_2023_J.Am.Chem.Soc_145_19243
Author(s) : Garcia-Meseguer R , Orti E , Tunon I , Ruiz-Pernia JJ , Arago J
Ref : Journal of the American Chemical Society , 145 :19243 , 2023
Abstract :
PubMedSearch : Garcia-Meseguer_2023_J.Am.Chem.Soc_145_19243
PubMedID: 37585687
Gene_locus related to this paper: idesa-peth

Title : On the Role of Temperature in the Depolymerization of PET by FAST-PETase: An Atomistic Point of View on Possible Active Site Pre-Organization and Substrate-Destabilization Effects - Orlando_2023_Chembiochem_24_e202300412
Author(s) : Orlando C , Prejano M , Russo N , Marino T
Ref : Chembiochem , 24 :e202300412 , 2023
Abstract :
PubMedSearch : Orlando_2023_Chembiochem_24_e202300412
PubMedID: 37556192
Gene_locus related to this paper: idesa-peth

Title : Complete Depolymerization of PET Wastes by an Evolved PET Hydrolase from Directed Evolution - Shi_2023_Angew.Chem.Int.Ed.Engl_62_e202218390
Author(s) : Shi L , Liu P , Tan Z , Zhao W , Gao J , Gu Q , Ma H , Liu H , Zhu L
Ref : Angew Chem Int Ed Engl , 62 :e202218390 , 2023
Abstract :
PubMedSearch : Shi_2023_Angew.Chem.Int.Ed.Engl_62_e202218390
PubMedID: 36751696
Gene_locus related to this paper: idesa-peth

Title : Conformational Selection of a Tryptophan Side Chain Drives the Generalized Increase in Activity of PET Hydrolases through a Ser\/Ile Double Mutation - Crnjar_2023_ACS.Org.Inorg.Au_3_109
Author(s) : Crnjar A , Grinen A , Kamerlin SCL , Ramirez-Sarmiento CA
Ref : ACS Org Inorg Au , 3 :109 , 2023
Abstract :
PubMedSearch : Crnjar_2023_ACS.Org.Inorg.Au_3_109
PubMedID: 37035283
Gene_locus related to this paper: idesa-peth

Title : Investigating the effects of cyclic topology on the performance of a plastic degrading enzyme for polyethylene terephthalate degradation - Hayes_2023_Sci.Rep_13_1267
Author(s) : Hayes HC , Luk LYP
Ref : Sci Rep , 13 :1267 , 2023
Abstract :
PubMedSearch : Hayes_2023_Sci.Rep_13_1267
PubMedID: 36690710
Gene_locus related to this paper: idesa-peth

Title : Improving the activity and thermostability of PETase from Ideonella sakaiensis through modulating its post-translational glycan modification - Deng_2023_Commun.Biol_6_39
Author(s) : Deng B , Yue Y , Yang J , Yang M , Xing Q , Peng H , Wang F , Li M , Ma L , Zhai C
Ref : Commun Biol , 6 :39 , 2023
Abstract :
PubMedSearch : Deng_2023_Commun.Biol_6_39
PubMedID: 36639437
Gene_locus related to this paper: idesa-peth

Title : Concentration-dependent inhibition of mesophilic PETases on poly(ethylene terephthalate) can be eliminated by enzyme engineering - Avilan_2023_ChemSusChem__e202202277
Author(s) : Avilan L , Lichtenstein BR , Koenig G , Zahn M , Allen MD , Oliveira L , Clark M , Bemmer V , Graham R , Austin HP , Dominick G , Johnson CW , Beckham GT , McGeehan J , Pickford AR
Ref : ChemSusChem , :e202202277 , 2023
Abstract :
PubMedSearch : Avilan_2023_ChemSusChem__e202202277
PubMedID: 36811288
Gene_locus related to this paper: psea4-u2z2l5 , 9gamm-a0a031mkr8 , 9burk-a0a1w6l438 , 9psed-a0a078mgg8 , pseol-e9kjl1 , 9burk-a0a0g3bi90 , 9burk-a0a1w6l588 , idesa-peth , acide-PBSA

Title : Rapid depolymerization of poly(ethylene terephthalate) thin films by a dual-enzyme system and its impact on material properties - Tarazona_2022_Chem.Catal_2_3573
Author(s) : Tarazona NA , Wei R , Brott S , Pfaff L , Bornscheuer UT , Lendlein A , Machatschek R
Ref : Chem Catal , 2 :3573 , 2022
Abstract :
PubMedSearch : Tarazona_2022_Chem.Catal_2_3573
PubMedID: 37350932
Gene_locus related to this paper: idesa-mheth , idesa-peth

Title : Directed evolution of an efficient and thermostable PET depolymerase - Bell_2022_Nat.Catal_5_673
Author(s) : Bell EL , Smithson R , Kilbride S , Foster J , Hardy FJ , Ramachandran S , Tedstone AA , Haigh SJ , Garforth AA , Day PJR , Levy C , Shaver MP , Green AP
Ref : Nature Catalysis , 5 :673 , 2022
Abstract :
PubMedSearch : Bell_2022_Nat.Catal_5_673
PubMedID:
Gene_locus related to this paper: idesa-peth

Title : Ancestral Sequence Reconstruction Identifies Structural Changes Underlying the Evolution of Ideonella sakaiensis PETase and Variants with Improved Stability and Activity - Joho_2022_Biochemistry__
Author(s) : Joho Y , Vongsouthi V , Spence MA , Ton J , Gomez C , Tan LL , Kaczmarski JA , Caputo AT , Royan S , Jackson CJ , Ardevol A
Ref : Biochemistry , : , 2022
Abstract :
PubMedSearch : Joho_2022_Biochemistry__
PubMedID: 35951410
Gene_locus related to this paper: idesa-peth

Title : In Silico Identification of Potential Sites for a Plastic-Degrading Enzyme by a Reverse Screening through the Protein Sequence Space and Molecular Dynamics Simulations - Charupanit_2022_Molecules_27_
Author(s) : Charupanit K , Tipmanee V , Sutthibutpong T , Limsakul P
Ref : Molecules , 27 : , 2022
Abstract :
PubMedSearch : Charupanit_2022_Molecules_27_
PubMedID: 35630830
Gene_locus related to this paper: idesa-peth

Title : Machine learning-aided engineering of hydrolases for PET depolymerization - Lu_2022_Nature_604_662
Author(s) : Lu H , Diaz DJ , Czarnecki NJ , Zhu C , Kim W , Shroff R , Acosta DJ , Alexander BR , Cole HO , Zhang Y , Lynd NA , Ellington AD , Alper HS
Ref : Nature , 604 :662 , 2022
Abstract :
PubMedSearch : Lu_2022_Nature_604_662
PubMedID: 35478237
Gene_locus related to this paper: idesa-peth

Title : Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin - Chen_2022_Nat.Commun_13_7138
Author(s) : Chen Z , Duan R , Xiao Y , Wei Y , Zhang H , Sun X , Wang S , Cheng Y , Wang X , Tong S , Yao Y , Zhu C , Yang H , Wang Y , Wang Z
Ref : Nat Commun , 13 :7138 , 2022
Abstract :
PubMedSearch : Chen_2022_Nat.Commun_13_7138
PubMedID: 36414665
Gene_locus related to this paper: idesa-peth

Title : Enhanced biodegradation of waste poly(ethylene terephthalate) using a reinforced plastic degrading enzyme complex - Hwang_2022_Sci.Total.Environ__156890
Author(s) : Hwang DH , Lee ME , Cho BH , Oh JW , You SK , Ko YJ , Hyeon JE , Han SO
Ref : Sci Total Environ , :156890 , 2022
Abstract :
PubMedSearch : Hwang_2022_Sci.Total.Environ__156890
PubMedID: 35753492
Gene_locus related to this paper: idesa-peth , canar-LipB

Title : Engineering and evaluation of thermostable IsPETase variants for PET degradation - Brott_2022_Eng.Life.Sci_22_192
Author(s) : Brott S , Pfaff L , Schuricht J , Schwarz JN , Bottcher D , Badenhorst CPS , Wei R , Bornscheuer UT
Ref : Eng Life Sciences , 22 :192 , 2022
Abstract :
PubMedSearch : Brott_2022_Eng.Life.Sci_22_192
PubMedID: 35382549
Gene_locus related to this paper: idesa-peth

Title : Machine Learning-Based Enzyme Engineering of PETase for Improved Efficiency in Degrading Non-Biodegradable Plastic - Gupta_2022_Biorxiv__
Author(s) : Gupta A , Agrawal S
Ref : Biorxiv , : , 2022
Abstract :
PubMedSearch : Gupta_2022_Biorxiv__
PubMedID:
Gene_locus related to this paper: idesa-peth

Title : Reaction Pathways for the Enzymatic Degradation of Poly(Ethylene Terephthalate): What Characterizes an Efficient PET-Hydrolase? - Schubert_2022_Chembiochem__e202200516
Author(s) : Schubert S , Schaller K , Baath JA , Hunt C , Borch K , Jensen K , Brask J , Westh P
Ref : Chembiochem , :e202200516 , 2022
Abstract :
PubMedSearch : Schubert_2022_Chembiochem__e202200516
PubMedID: 36399069
Gene_locus related to this paper: idesa-peth , humin-cut , 9bact-g9by57 , thefu-q6a0i4

Title : Overexpression and kinetic analysis of Ideonella sakaiensis PETase for polyethylene terephthalate (PET) degradation - Aer_2022_Environ.Res_212_113472
Author(s) : Aer L , Jiang Q , Gul I , Qi Z , Feng J , Tang L
Ref : Environ Research , 212 :113472 , 2022
Abstract :
PubMedSearch : Aer_2022_Environ.Res_212_113472
PubMedID: 35577005
Gene_locus related to this paper: idesa-peth

Title : QM\/MM Investigation to Identify the Hallmarks of Superior PET Biodegradation Activity of PETase over Cutinase - Aboelnga_2022_ACS.Sustain.Chem.Eng_10_15857
Author(s) : Aboelnga MM , Kalyaanamoorthy S
Ref : ACS Sustain Chem Eng , 10 :15857 , 2022
Abstract :
PubMedSearch : Aboelnga_2022_ACS.Sustain.Chem.Eng_10_15857
PubMedID:
Gene_locus related to this paper: idesa-peth , thefu-q6a0i4

Title : Comparative performance of PETase as a function of reaction conditions, substrate properties, and product accumulation - Erickson_2022_ChemSusChem_15_e202101932
Author(s) : Erickson E , Shakespeare TJ , Bratti F , Buss BL , Graham R , Hawkins MA , Konig G , Michener WE , Miscall J , Ramirez KJ , Rorrer NA , Zahn M , Pickford AR , McGeehan JE , Beckham G
Ref : ChemSusChem , 15 : , 2022
Abstract :
PubMedSearch : Erickson_2022_ChemSusChem_15_e202101932
PubMedID: 34587366
Gene_locus related to this paper: idesa-peth

Title : Directed Evolution of an Efficient and Thermostable PET Depolymerase - Bell_2021_Chemrxiv__
Author(s) : Bell E , Smithson R , Kilbride S , Foster J , Hardy F , Ramachandran S , Tedstone A , Haigh S , Garforth A , Day P , Levy C , Shaver M , Green A
Ref : Chemrxiv , : , 2021
Abstract :
PubMedSearch : Bell_2021_Chemrxiv__
PubMedID:
Gene_locus related to this paper: idesa-peth

Title : Computational redesign of a PETase for plastic biodegradation under ambient condition by the GRAPE strategy - Cui_2021_ACS.Catal_11_1340
Author(s) : Cui Y , Chen Y , Liu X , Dong S , Tian Y , Qiao Y , Mitra R , Han J , Li C , Han X
Ref : ACS Catal , 11 :1340 , 2021
Abstract :
PubMedSearch : Cui_2021_ACS.Catal_11_1340
PubMedID:
Gene_locus related to this paper: idesa-peth

Title : Reaction Mechanism of the PET Degrading Enzyme PETase Studied with DFT\/MM Molecular Dynamics Simulations - Jerves_2021_ACS.Catal_11_11626
Author(s) : Jerves C , Neves RPP , Ramos MJ , da Silva S , Fernandes PA
Ref : ACS Catal , 11 :11626 , 2021
Abstract :
PubMedSearch : Jerves_2021_ACS.Catal_11_11626
PubMedID:
Gene_locus related to this paper: idesa-peth

Title : An Efficient Protein Evolution Workflow for the Improvement of Bacterial PET Hydrolyzing Enzymes - Pirillo_2021_Int.J.Mol.Sci_23_
Author(s) : Pirillo V , Orlando M , Tessaro D , Pollegioni L , Molla G
Ref : Int J Mol Sci , 23 : , 2021
Abstract :
PubMedSearch : Pirillo_2021_Int.J.Mol.Sci_23_
PubMedID: 35008691
Gene_locus related to this paper: idesa-peth

Title : Perspectives on the Role of Enzymatic Biocatalysis for the Degradation of Plastic PET - Magalhaes_2021_Int.J.Mol.Sci_22_11257
Author(s) : Magalhaes RP , Cunha JM , Sousa SF
Ref : Int J Mol Sci , 22 :11257 , 2021
Abstract :
PubMedSearch : Magalhaes_2021_Int.J.Mol.Sci_22_11257
PubMedID: 34681915
Gene_locus related to this paper: 9entr-EsEstB , 9bact-a0a2h5z9r5 , 9psed-peh , 9actn-h6wx58 , idesa-mheth , idesa-peth , thecd-d1a2h1 , humin-cut , 9acto-d4q9n1 , 9acto-f7ix06 , 9bact-g9by57 , bacsu-lip , bacsu-pnbae , canar-LipB , thela-m4tp71 , psemy-a4y035 , thefu-1831 , thefu-q6a0i4 , strsw-c9zcr8 , fusox-CUT , sacvd-c7mve8

Title : Deep learning redesign of PETase for practical PET degrading applications - Lu_2021_Biorxiv__
Author(s) : Lu H , Diaz DJ , Czarnecki NJ , Zhu C , Kim W , Shroff R , Acosta DJ , Alexander B , Cole H , Zhang YJ , Lynd N , Ellington AD , Alper HS
Ref : Biorxiv , : , 2021
Abstract :
PubMedSearch : Lu_2021_Biorxiv__
PubMedID:
Gene_locus related to this paper: idesa-peth

Title : General features to enhance enzymatic activity of poly(ethylene terephthalate) hydrolysis - Chen_2021_Nat.Catal_4_425
Author(s) : Chen CC , Han X , Li X , Jiang P , Niu D , Ma L , Liu W , Li S , Qu Y , Hu H , Min J , Yang Y , Zhang L , Zeng W , Huang JW , Dai L , Guo RT , Chen, CC
Ref : Nature Catalysis , 4 :425 , 2021
Abstract :
PubMedSearch : Chen_2021_Nat.Catal_4_425
PubMedID:
Gene_locus related to this paper: 9burk-a0a1f4jxw8 , idesa-peth

Title : Adsorption of enzymes with hydrolytic activity on polyethylene terephthalate - Badino_2021_Enzyme.Microb.Technol_152_109937
Author(s) : Badino SF , Baath JA , Borch K , Jensen K , Westh P
Ref : Enzyme Microb Technol , 152 :109937 , 2021
Abstract :
PubMedSearch : Badino_2021_Enzyme.Microb.Technol_152_109937
PubMedID: 34749019
Gene_locus related to this paper: idesa-peth , humin-cut , thefu-q6a0i4

Title : Surface display as a functional screening platform for detecting enzymes active on PET - Heyde_2021_Microb.Cell.Fact_20_93
Author(s) : Heyde SAH , Arnling Baath J , Westh P , Norholm MHH , Jensen K
Ref : Microb Cell Fact , 20 :93 , 2021
Abstract :
PubMedSearch : Heyde_2021_Microb.Cell.Fact_20_93
PubMedID: 33933097
Gene_locus related to this paper: idesa-peth

Title : QM\/MM Study of the Enzymatic Biodegradation Mechanism of Polyethylene Terephthalate - Boneta_2021_J.Chem.Inf.Model__
Author(s) : Boneta S , Arafet K , Moliner V
Ref : J Chem Inf Model , : , 2021
Abstract :
PubMedSearch : Boneta_2021_J.Chem.Inf.Model__
PubMedID: 34085821
Gene_locus related to this paper: idesa-peth , 9bact-g9by57

Title : Assessment of the PETase conformational changes induced by poly(ethylene terephthalate) binding - da Costa_2021_Proteins__
Author(s) : da Costa CHS , Dos Santos AM , Alves CN , Marti S , Moliner V , Santana K , Lameira J
Ref : Proteins , : , 2021
Abstract :
PubMedSearch : da Costa_2021_Proteins__
PubMedID: 34075621
Gene_locus related to this paper: idesa-peth

Title : Yeast cell surface display of bacterial PET hydrolase as a sustainable biocatalyst for the degradation of polyethylene terephthalate - Chen_2021_Methods.Enzymol_648_457
Author(s) : Chen Z , Xiao Y , Weber G , Wei R , Wang Z
Ref : Methods Enzymol , 648 :457 , 2021
Abstract :
PubMedSearch : Chen_2021_Methods.Enzymol_648_457
PubMedID: 33579416
Gene_locus related to this paper: idesa-peth

Title : Enhancing PET hydrolytic enzyme activity by fusion of the cellulose-binding domain of cellobiohydrolase I from Trichoderma reesei - Dai_2021_J.Biotechnol_334_47
Author(s) : Dai L , Qu Y , Huang JW , Hu Y , Hu H , Li S , Chen CC , Guo RT
Ref : J Biotechnol , 334 :47 , 2021
Abstract :
PubMedSearch : Dai_2021_J.Biotechnol_334_47
PubMedID: 34044062
Gene_locus related to this paper: idesa-peth

Title : Protein engineering of stable IsPETase for PET plastic degradation by Premuse - Meng_2021_Int.J.Biol.Macromol_180_667
Author(s) : Meng X , Yang L , Liu H , Li Q , Xu G , Zhang Y , Guan F , Zhang W , Wu N , Tian J
Ref : Int J Biol Macromol , 180 :667 , 2021
Abstract :
PubMedSearch : Meng_2021_Int.J.Biol.Macromol_180_667
PubMedID: 33753197
Gene_locus related to this paper: idesa-peth

Title : Class I hydrophobins pretreatment stimulates PETase for monomers recycling of waste PETs - Puspitasari_2021_Int.J.Biol.Macromol_176_157
Author(s) : Puspitasari N , Tsai SL , Lee CK
Ref : Int J Biol Macromol , 176 :157 , 2021
Abstract :
PubMedSearch : Puspitasari_2021_Int.J.Biol.Macromol_176_157
PubMedID: 33561457
Gene_locus related to this paper: idesa-peth

Title : Enhanced Extracellular Production of IsPETase in Escherichia coli via Engineering of the pelB Signal Peptide - Shi_2021_J.Agric.Food.Chem_69_2245
Author(s) : Shi L , Liu H , Gao S , Weng Y , Zhu L
Ref : Journal of Agricultural and Food Chemistry , 69 :2245 , 2021
Abstract :
PubMedSearch : Shi_2021_J.Agric.Food.Chem_69_2245
PubMedID: 33576230
Gene_locus related to this paper: idesa-peth

Title : GRAPE, a greedy accumulated strategy for computational protein engineering - Sun_2021_Methods.Enzymol_648_207
Author(s) : Sun J , Cui Y , Wu B
Ref : Methods Enzymol , 648 :207 , 2021
Abstract :
PubMedSearch : Sun_2021_Methods.Enzymol_648_207
PubMedID: 33579404
Gene_locus related to this paper: idesa-peth

Title : An absorbance method for analysis of enzymatic degradation kinetics of poly(ethylene terephthalate) films - Zhong-Johnson_2021_Sci.Rep_11_928
Author(s) : Zhong-Johnson EZL , Voigt CA , Sinskey AJ
Ref : Sci Rep , 11 :928 , 2021
Abstract :
PubMedSearch : Zhong-Johnson_2021_Sci.Rep_11_928
PubMedID: 33441590
Gene_locus related to this paper: idesa-peth

Title : Structural analysis of PET-degrading enzymes PETase and MHETase from Ideonella sakaiensis - Graf_2021_Methods.Enzymol_648_337
Author(s) : Graf LG , Michels EAP , Yew Y , Liu W , Palm GJ , Weber G
Ref : Methods Enzymol , 648 :337 , 2021
Abstract :
PubMedSearch : Graf_2021_Methods.Enzymol_648_337
PubMedID: 33579411
Gene_locus related to this paper: idesa-mheth , idesa-peth

Title : Development of a targeted gene disruption system in the PET-degrading bacterium Ideonella sakaiensis and its applications to PETase and MHETase genes - Hachisuka_2021_Appl.Environ.Microbiol__AEM0002021
Author(s) : Hachisuka SI , Nishii T , Yoshida S
Ref : Applied Environmental Microbiology , :AEM0002021 , 2021
Abstract :
PubMedSearch : Hachisuka_2021_Appl.Environ.Microbiol__AEM0002021
PubMedID: 34260304
Gene_locus related to this paper: idesa-mheth , idesa-peth

Title : Tandem chemical deconstruction and biological upcycling of poly(ethylene terephthalate) to beta-ketoadipic acid by Pseudomonas putida KT2440 - Werner_2021_Metab.Eng_67_250
Author(s) : Werner AZ , Clare R , Mand TD , Pardo I , Ramirez KJ , Haugen SJ , Bratti F , Dexter GN , Elmore JR , Huenemann JD , Peabody GLt , Johnson CW , Rorrer NA , Salvachua D , Guss AM , Beckham GT
Ref : Metab Eng , 67 :250 , 2021
Abstract :
PubMedSearch : Werner_2021_Metab.Eng_67_250
PubMedID: 34265401
Gene_locus related to this paper: idesa-mheth , idesa-peth

Title : Ideonella sakaiensis, PETase, and MHETase: From identification of microbial PET degradation to enzyme characterization - Yoshida_2021_Methods.Enzymol_648_187
Author(s) : Yoshida S , Hiraga K , Taniguchi I , Oda K
Ref : Methods Enzymol , 648 :187 , 2021
Abstract :
PubMedSearch : Yoshida_2021_Methods.Enzymol_648_187
PubMedID: 33579403
Gene_locus related to this paper: idesa-mheth , idesa-peth

Title : Comparative biochemistry of four polyester (PET) hydrolases - Baath_2020_Chembiochem_22_1627
Author(s) : Baath JA , Borch K , Jensen K , Brask J , Westh P
Ref : Chembiochem , 22 :1627 , 2020
Abstract :
PubMedSearch : Baath_2020_Chembiochem_22_1627
PubMedID: 33351214
Gene_locus related to this paper: idesa-peth , humin-cut , bacsu-pnbae , thefu-q6a0i4 , thefu-q6a0i3

Title : Computational redesign of a PETase for plastic biodegradation by the GRAPE strategy - Cui_2020_Biorxiv__
Author(s) : Cui YL , Chen YC , Liu XY , Dong SJ , Han J , Xiang H , Chen Q , Liu HY , Han X , Liu WD , Tang SY , Wu B
Ref : Biorxiv , : , 2020
Abstract :
PubMedSearch : Cui_2020_Biorxiv__
PubMedID:
Gene_locus related to this paper: idesa-peth

Title : Recent advances in biocatalysts engineering for polyethylene terephthalate plastic waste green recycling - Samak_2020_Environ.Int_145_106144
Author(s) : Samak NA , Jia Y , Sharshar MM , Mu T , Yang M , Peh S , Xing J
Ref : Environ Int , 145 :106144 , 2020
Abstract :
PubMedSearch : Samak_2020_Environ.Int_145_106144
PubMedID: 32987219
Gene_locus related to this paper: idesa-peth , 9bact-g9by57

Title : Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis - Liu_2019_Biochem.Biophys.Res.Commun_508_289
Author(s) : Liu C , Shi C , Zhu S , Wei R , Yin CC
Ref : Biochemical & Biophysical Research Communications , 508 :289 , 2019
Abstract :
PubMedSearch : Liu_2019_Biochem.Biophys.Res.Commun_508_289
PubMedID: 30502092
Gene_locus related to this paper: idesa-peth

Title : Biodegradation of waste PET: A sustainable solution for dealing with plastic pollution - Hiraga_2019_EMBO.Rep_20_e49365
Author(s) : Hiraga K , Taniguchi I , Yoshida S , Kimura Y , Oda K
Ref : EMBO Rep , 20 :e49365 , 2019
Abstract :
PubMedSearch : Hiraga_2019_EMBO.Rep_20_e49365
PubMedID: 31646721
Gene_locus related to this paper: idesa-peth

Title : Rational Protein Engineering of Thermo-Stable PETase from Ideonella sakaiensis for Highly Efficient PET Degradation - Son_2019_ACS.Catal_9_3519
Author(s) : Son HF , Cho IJ , Joo S , Seo H , Sagong HY , Choi SY , Lee SY , Kim KJ
Ref : ACS Catal , 9 :3519 , 2019
Abstract :
PubMedSearch : Son_2019_ACS.Catal_9_3519
PubMedID:
Gene_locus related to this paper: idesa-mheth , idesa-peth

Title : Enhanced Poly(ethylene terephthalate) Hydrolase Activity by Protein Engineering - Ma_2018_Engineering.(Beijing)_4_888
Author(s) : Ma Y , Yao M , Li B , Ding M , He B , Chen S , Zhou X , Yuan Y
Ref : Engineering (Beijing) , 4 :888 , 2018
Abstract :
PubMedSearch : Ma_2018_Engineering.(Beijing)_4_888
PubMedID:
Gene_locus related to this paper: idesa-peth

Title : Active Site Flexibility as a Hallmark for Efficient PET Degradation by I. sakaiensis PETase - Fecker_2018_Biophys.J_114_1302
Author(s) : Fecker T , Galaz-Davison P , Engelberger F , Narui Y , Sotomayor M , Parra LP , Ramirez-Sarmiento CA
Ref : Biophysical Journal , 114 :1302 , 2018
Abstract :
PubMedSearch : Fecker_2018_Biophys.J_114_1302
PubMedID: 29590588
Gene_locus related to this paper: idesa-peth

Title : Characterization and engineering of a plastic-degrading aromatic polyesterase - Austin_2018_Proc.Natl.Acad.Sci.U.S.A_115_E4350
Author(s) : Austin HP , Allen MD , Donohoe BS , Rorrer NA , Kearns FL , Silveira RL , Pollard BC , Dominick G , Duman R , El Omari K , Mykhaylyk V , Wagner A , Michener WE , Amore A , Skaf MS , Crowley MF , Thorne AW , Johnson CW , Woodcock HL , McGeehan JE , Beckham GT
Ref : Proc Natl Acad Sci U S A , 115 :E4350 , 2018
Abstract :
PubMedSearch : Austin_2018_Proc.Natl.Acad.Sci.U.S.A_115_E4350
PubMedID: 29666242
Gene_locus related to this paper: idesa-peth

Title : Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation - Joo_2018_Nat.Commun_9_382
Author(s) : Joo S , Cho IJ , Seo H , Son HF , Sagong HY , Shin TJ , Choi SY , Lee SY , Kim KJ
Ref : Nat Commun , 9 :382 , 2018
Abstract :
PubMedSearch : Joo_2018_Nat.Commun_9_382
PubMedID: 29374183
Gene_locus related to this paper: idesa-peth

Title : Protein Crystallography and Site-Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis - Liu_2018_Chembiochem_19_1471
Author(s) : Liu B , He L , Wang L , Li T , Li C , Liu H , Luo Y , Bao R
Ref : Chembiochem , 19 :1471 , 2018
Abstract :
PubMedSearch : Liu_2018_Chembiochem_19_1471
PubMedID: 29603535
Gene_locus related to this paper: idesa-peth

Title : New insights into the function and global distribution of polyethylene terephthalate (PET) degrading bacteria and enzymes in marine and terrestrial metagenomes - Danso_2018_Appl.Environ.Microbiol_84_e2773
Author(s) : Danso D , Schmeisser C , Chow J , Zimmermann W , Wei R , Leggewie C , Li X , Hazen T , Streit WR
Ref : Applied Environmental Microbiology , 84 :e2773 , 2018
Abstract :
PubMedSearch : Danso_2018_Appl.Environ.Microbiol_84_e2773
PubMedID: 29427431
Gene_locus related to this paper: 9burk-PET10 , 9burk-PET11 , 9gamm-a0a0d4l7e6 , 9alte-n6vy44 , 9zzzz-a0a0f9x315 , deiml-e8u721 , olean-r4ykl9 , vibga-a0a1z2siq1 , 9burk-a0a0g3bi90 , 9bact-c3ryl0 , 9actn-h6wx58 , idesa-peth , 9bact-g9by57 , acide-PBSA , morsp-lip1

Title : Structural insight into catalytic mechanism of PET hydrolase - Han_2017_Nat.Commun_8_2106
Author(s) : Han X , Liu W , Huang JW , Ma J , Zheng Y , Ko TP , Xu L , Cheng YS , Chen CC , Guo RT
Ref : Nat Commun , 8 :2106 , 2017
Abstract :
PubMedSearch : Han_2017_Nat.Commun_8_2106
PubMedID: 29235460
Gene_locus related to this paper: idesa-peth

Title : Ideonella sakaiensis sp. nov., isolated from a microbial consortium that degrades poly(ethylene terephthalate) - Tanasupawat_2016_Int.J.Syst.Evol.Microbiol_66_2813
Author(s) : Tanasupawat S , Takehana T , Yoshida S , Hiraga K , Oda K
Ref : Int J Syst Evol Microbiol , 66 :2813 , 2016
Abstract :
PubMedSearch : Tanasupawat_2016_Int.J.Syst.Evol.Microbiol_66_2813
PubMedID: 27045688
Gene_locus related to this paper: idesa-peth

Title : Comment on A bacterium that degrades and assimilates poly(ethylene terephthalate) - Yang_2016_Science_353_759
Author(s) : Yang Y , Yang J , Jiang L
Ref : Science , 353 :759 , 2016
Abstract :
PubMedSearch : Yang_2016_Science_353_759
PubMedID: 27540159
Gene_locus related to this paper: idesa-peth

Title : Response to Comment on A bacterium that degrades and assimilates poly(ethylene terephthalate) - Yoshida_2016_Science_353_759
Author(s) : Yoshida S , Hiraga K , Takehana T , Taniguchi I , Yamaji H , Maeda Y , Toyohara K , Miyamoto K , Kimura Y , Oda K
Ref : Science , 353 :759 , 2016
Abstract :
PubMedSearch : Yoshida_2016_Science_353_759
PubMedID: 27540160
Gene_locus related to this paper: idesa-peth

Title : A bacterium that degrades and assimilates poly(ethylene terephthalate) - Yoshida_2016_Science_351_1196
Author(s) : Yoshida S , Hiraga K , Takehana T , Taniguchi I , Yamaji H , Maeda Y , Toyohara K , Miyamoto K , Kimura Y , Oda K
Ref : Science , 351 :1196 , 2016
Abstract :
PubMedSearch : Yoshida_2016_Science_351_1196
PubMedID: 26965627
Gene_locus related to this paper: idesa-mheth , idesa-peth