This family differs substantially from the cutinase acetyl-xylan esterase family (cutinase monofunctional). Several cutinases from the genus Thermobifida act on biodegradable plastics such as synthetic polyesters. Not all cutinases can degrade polyester plastics. Aerial plant organs are protected by a cuticle composed of an insoluble polymeric structural compound, cutin, which is a polyester composed of hydroxy and hydroxyepoxy fatty acids. Cutinases are lipases with a specificity for p-nitrophenyl acyl esters with short chain acyl group. This family was extracted from the Bacterial_lipase family which is close to PAF-Acetylhydrolase family. Streptomyces exfoliatus lipase (1JFR) Pseudomonas mendocina lipase (2FX5) are included in this family. This family correspond to family III of the classification of Arpigny et al 1999. Polyethylene terephthalate degrading hydrolase/PET-hydrolase/PET Hydrolase (type II PETase). Two enzymes in Ideonella sakaiensis (for example) act on PET (Poly ethylene terephthalate): idesa-peth from Polyesterase-lipase-cutinase family and idesa-mheth which acts on extremity of PET (Exo-PETase Function PET hydrolase PET-Hydrolase) and on MHET the product of hydrolysis of PET. MHETase belongs to the Tannase family
Interpro : IPR041127 Chlorophyllase enzyme
PIRSF : No PIRSF
Pdoc : No Pdoc
Pfam : PF12695 Abhydrolase_5 , PF12740 Chlorophyllase2
Prints : No Print
EC Number : 3.1.1.74
Structures (146)
Genes Proteins in Polyesterase-lipase-cutinase family (191)
No fragment of genes
Structures in Polyesterase-lipase-cutinase family (146)Substrates in Polyesterase-lipase-cutinase family (40)
Inhibitors in Polyesterase-lipase-cutinase family (7)
Title : Recent advances in microbial and enzymatic engineering for the biodegradation of micro- and nanoplastics - Choi_2024_RSC.Adv_14_9943 |
Author(s) : Choi J , Kim H , Ahn YR , Kim M , Yu S , Kim N , Lim SY , Park JA , Ha SJ , Lim KS , Kim HO |
Ref : RSC Adv , 14 :9943 , 2024 |
Abstract : Choi_2024_RSC.Adv_14_9943 |
ESTHER : Choi_2024_RSC.Adv_14_9943 |
PubMedSearch : Choi_2024_RSC.Adv_14_9943 |
PubMedID: 38528920 |
Title : The structural and molecular mechanisms of type II PETases: a mini review - Duan_2023_Biotechnol.Lett__ |
Author(s) : Duan S , Zhang N , Chao T , Wu Y , Wang M |
Ref : Biotechnol Lett , : , 2023 |
Abstract : Duan_2023_Biotechnol.Lett__ |
ESTHER : Duan_2023_Biotechnol.Lett__ |
PubMedSearch : Duan_2023_Biotechnol.Lett__ |
PubMedID: 37535135 |
Title : Discovery and Genetic Code Expansion of a Polyethylene Terephthalate (PET) Hydrolase from the Human Saliva Metagenome for the Degradation and Bio-Functionalization of PET - Eiamthong_2022_Angew.Chem.Int.Ed.Engl_15_e202203061 |
Author(s) : 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 MM , Chin JW , Pakotiprapha D , Bhanthumnavin W , Uttamapinant C |
Ref : Angew Chem Int Ed Engl , :e202203061 , 2022 |
Abstract : Eiamthong_2022_Angew.Chem.Int.Ed.Engl_15_e202203061 |
ESTHER : Eiamthong_2022_Angew.Chem.Int.Ed.Engl_15_e202203061 |
PubMedSearch : Eiamthong_2022_Angew.Chem.Int.Ed.Engl_15_e202203061 |
PubMedID: 35656865 |
Gene_locus related to this paper: 9gamm-PETaseMG1 , 9gamm-PETaseMG2 , 9gamm-PETaseMG3 , 9gamm-PETaseMG4 , 9gamm-PETaseMG5 , 9gamm-PETaseMG6 , 9gamm-PETaseMG7 , 9gamm-PETaseMG8 , 9pseu-PETaseMG9 , 9actn-PETaseMG10 |
Title : Plastics degradation by hydrolytic enzymes: The plastics-active enzymes database-PAZy - Buchholz_2022_Proteins_90_1443 |
Author(s) : Buchholz PCF , Feuerriegel G , Zhang H , Perez-Garcia P , Nover LL , Chow J , Streit WR , Pleiss J |
Ref : Proteins , 90 :1443 , 2022 |
Abstract : Buchholz_2022_Proteins_90_1443 |
ESTHER : Buchholz_2022_Proteins_90_1443 |
PubMedSearch : Buchholz_2022_Proteins_90_1443 |
PubMedID: 35175626 |
Title : Positive Charge Introduction on the Surface of Thermostabilized PET Hydrolase Facilitates PET Binding and Degradation - Nakamura_2021_ACS.Catal_11_8550 |
Author(s) : Nakamura A , Kobayashi N , Koga N , Iino R |
Ref : ACS Catal , 11 :8550 , 2021 |
Abstract : Nakamura_2021_ACS.Catal_11_8550 |
ESTHER : Nakamura_2021_ACS.Catal_11_8550 |
PubMedSearch : Nakamura_2021_ACS.Catal_11_8550 |
PubMedID: |
Gene_locus related to this paper: 9bact-c3ryl0 |
Title : Implications for the PET decomposition mechanism through similarity and dissimilarity between PETases from Rhizobacter gummiphilus and Ideonella sakaiensis - Sagong_2021_J.Hazard.Mater_416_126075 |
Author(s) : Sagong HY , Son HF , Seo H , Hong H , Lee D , Kim KJ |
Ref : J Hazard Mater , 416 :126075 , 2021 |
Abstract : Sagong_2021_J.Hazard.Mater_416_126075 |
ESTHER : Sagong_2021_J.Hazard.Mater_416_126075 |
PubMedSearch : Sagong_2021_J.Hazard.Mater_416_126075 |
PubMedID: 34492896 |
Gene_locus related to this paper: 9burk-a0a1w6l588 |
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 : Heyde_2021_Microb.Cell.Fact_20_93 |
ESTHER : Heyde_2021_Microb.Cell.Fact_20_93 |
PubMedSearch : Heyde_2021_Microb.Cell.Fact_20_93 |
PubMedID: 33933097 |
Gene_locus related to this paper: idesa-peth |
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 : da Costa_2021_Proteins__ |
ESTHER : da Costa_2021_Proteins__ |
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 : Chen_2021_Methods.Enzymol_648_457 |
ESTHER : Chen_2021_Methods.Enzymol_648_457 |
PubMedSearch : Chen_2021_Methods.Enzymol_648_457 |
PubMedID: 33579416 |
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 : Chen_2021_Nat.Catal_4_425 |
ESTHER : Chen_2021_Nat.Catal_4_425 |
PubMedSearch : Chen_2021_Nat.Catal_4_425 |
PubMedID: |
Gene_locus related to this paper: 9burk-a0a1f4jxw8 , 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 : Dai_2021_J.Biotechnol_334_47 |
ESTHER : Dai_2021_J.Biotechnol_334_47 |
PubMedSearch : Dai_2021_J.Biotechnol_334_47 |
PubMedID: 34044062 |
Gene_locus related to this paper: idesa-peth |
Title : Novel Pet-Degrading Enzymes: Structure-Function from a Computational Perspective - Berselli_2021_Chembiochem_22_2032 |
Author(s) : Berselli A , Ramos MJ , Menziani MC |
Ref : Chembiochem , 22 :2032 , 2021 |
Abstract : Berselli_2021_Chembiochem_22_2032 |
ESTHER : Berselli_2021_Chembiochem_22_2032 |
PubMedSearch : Berselli_2021_Chembiochem_22_2032 |
PubMedID: 33470503 |
Title : Structural Insights into Carboxylic Polyester-Degrading Enzymes and Their Functional Depolymerizing Neighbors - Leitao_2021_Int.J.Mol.Sci_22_ |
Author(s) : Leitao AL , Enguita FJ |
Ref : Int J Mol Sci , 22 : , 2021 |
Abstract : Leitao_2021_Int.J.Mol.Sci_22_ |
ESTHER : Leitao_2021_Int.J.Mol.Sci_22_ |
PubMedSearch : Leitao_2021_Int.J.Mol.Sci_22_ |
PubMedID: 33652738 |
Title : Emerging Roles of PETase and MHETase in the Biodegradation of Plastic Wastes - Maity_2021_Appl.Biochem.Biotechnol_193_2699 |
Author(s) : Maity W , Maity S , Bera S , Roy A |
Ref : Appl Biochem Biotechnol , 193 :2699 , 2021 |
Abstract : Maity_2021_Appl.Biochem.Biotechnol_193_2699 |
ESTHER : Maity_2021_Appl.Biochem.Biotechnol_193_2699 |
PubMedSearch : Maity_2021_Appl.Biochem.Biotechnol_193_2699 |
PubMedID: 33797026 |
Title : Structural basis for Ca(2+)-dependent catalysis of a cutinase-like enzyme and its engineering: application to enzymatic PET depolymerization - Oda_2021_Biophys.Physicobiol_18_168 |
Author(s) : Oda M |
Ref : Biophys Physicobiol , 18 :168 , 2021 |
Abstract : Oda_2021_Biophys.Physicobiol_18_168 |
ESTHER : Oda_2021_Biophys.Physicobiol_18_168 |
PubMedSearch : Oda_2021_Biophys.Physicobiol_18_168 |
PubMedID: 34386313 |
Gene_locus related to this paper: sacvd-c7mve8 |
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 : Graf_2021_Methods.Enzymol_648_337 |
ESTHER : Graf_2021_Methods.Enzymol_648_337 |
PubMedSearch : Graf_2021_Methods.Enzymol_648_337 |
PubMedID: 33579411 |
Gene_locus related to this paper: idesa-mheth , idesa-peth |
Title : Microbial Polyethylene Terephthalate Hydrolases: Current and Future Perspectives - Carr_2020_Front.Microbiol_11_571265 |
Author(s) : Carr CM , Clarke DJ , Dobson ADW |
Ref : Front Microbiol , 11 :571265 , 2020 |
Abstract : Carr_2020_Front.Microbiol_11_571265 |
ESTHER : Carr_2020_Front.Microbiol_11_571265 |
PubMedSearch : Carr_2020_Front.Microbiol_11_571265 |
PubMedID: 33262744 |
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 : Hiraga_2019_EMBO.Rep_20_e49365 |
ESTHER : Hiraga_2019_EMBO.Rep_20_e49365 |
PubMedSearch : Hiraga_2019_EMBO.Rep_20_e49365 |
PubMedID: 31646721 |
Gene_locus related to this paper: idesa-peth |
Title : PMBD: a Comprehensive Plastics Microbial Biodegradation Database - Gan_2019_Database.(Oxford)_2019_bav119 |
Author(s) : Gan Z , Zhang H |
Ref : Database (Oxford) , 2019 :bav119 , 2019 |
Abstract : Gan_2019_Database.(Oxford)_2019_bav119 |
ESTHER : Gan_2019_Database.(Oxford)_2019_bav119 |
PubMedSearch : Gan_2019_Database.(Oxford)_2019_bav119 |
PubMedID: 31738435 |
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 : Fecker_2018_Biophys.J_114_1302 |
ESTHER : Fecker_2018_Biophys.J_114_1302 |
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 : Austin_2018_Proc.Natl.Acad.Sci.U.S.A_115_E4350 |
ESTHER : Austin_2018_Proc.Natl.Acad.Sci.U.S.A_115_E4350 |
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 : Joo_2018_Nat.Commun_9_382 |
ESTHER : Joo_2018_Nat.Commun_9_382 |
PubMedSearch : Joo_2018_Nat.Commun_9_382 |
PubMedID: 29374183 |
Gene_locus related to this paper: idesa-peth |
Title : Structural studies reveal the molecular mechanism of PETase - Chen_2018_FEBS.J_285_3717 |
Author(s) : Chen CC , Han X , Ko TP , Liu W , Guo RT |
Ref : Febs J , 285 :3717 , 2018 |
Abstract : Chen_2018_FEBS.J_285_3717 |
ESTHER : Chen_2018_FEBS.J_285_3717 |
PubMedSearch : Chen_2018_FEBS.J_285_3717 |
PubMedID: 30048043 |
Title : Structural Dynamics of the PET-Degrading Cutinase-like Enzyme from Saccharomonospora viridis AHK190 in Substrate-Bound States Elucidates the Ca(2+)-Driven Catalytic Cycle - Numoto_2018_Biochemistry_57_5289 |
Author(s) : Numoto N , Kamiya N , Bekker GJ , Yamagami Y , Inaba S , Ishii K , Uchiyama S , Kawai F , Ito N , Oda M |
Ref : Biochemistry , 57 :5289 , 2018 |
Abstract : Numoto_2018_Biochemistry_57_5289 |
ESTHER : Numoto_2018_Biochemistry_57_5289 |
PubMedSearch : Numoto_2018_Biochemistry_57_5289 |
PubMedID: 30110540 |
Gene_locus related to this paper: sacvd-c7mve8 |
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 : Han_2017_Nat.Commun_8_2106 |
ESTHER : Han_2017_Nat.Commun_8_2106 |
PubMedSearch : Han_2017_Nat.Commun_8_2106 |
PubMedID: 29235460 |
Gene_locus related to this paper: idesa-peth |
Title : Small cause, large effect: Structural characterization of cutinases from Thermobifida cellulosilytica - Ribitsch_2017_Biotechnol.Bioeng_114_2481 |
Author(s) : Ribitsch D , Hromic A , Zitzenbacher S , Zartl B , Gamerith C , Pellis A , Jungbauer A , Lyskowski A , Steinkellner G , Gruber K , Tscheliessnig R , Herrero Acero E , Guebitz GM |
Ref : Biotechnol Bioeng , 114 :2481 , 2017 |
Abstract : Ribitsch_2017_Biotechnol.Bioeng_114_2481 |
ESTHER : Ribitsch_2017_Biotechnol.Bioeng_114_2481 |
PubMedSearch : Ribitsch_2017_Biotechnol.Bioeng_114_2481 |
PubMedID: 28671263 |
Gene_locus related to this paper: thefu-q6a0i4 , thefu-q6a0i3 |
Title : Structural basis for the Ca(2+)-enhanced thermostability and activity of PET-degrading cutinase-like enzyme from Saccharomonospora viridis AHK190 - Miyakawa_2015_Appl.Microbiol.Biotechnol_99_4297 |
Author(s) : Miyakawa T , Mizushima H , Ohtsuka J , Oda M , Kawai F , Tanokura M |
Ref : Applied Microbiology & Biotechnology , 99 :4297 , 2015 |
Abstract : Miyakawa_2015_Appl.Microbiol.Biotechnol_99_4297 |
ESTHER : Miyakawa_2015_Appl.Microbiol.Biotechnol_99_4297 |
PubMedSearch : Miyakawa_2015_Appl.Microbiol.Biotechnol_99_4297 |
PubMedID: 25492421 |
Gene_locus related to this paper: sacvd-c7mve8 |
Title : Synthetic polyester-hydrolyzing enzymes from thermophilic actinomycetes - Wei_2014_Adv.Appl.Microbiol_89_267 |
Author(s) : Wei R , Oeser T , Zimmermann W |
Ref : Adv Appl Microbiol , 89 :267 , 2014 |
Abstract : Wei_2014_Adv.Appl.Microbiol_89_267 |
ESTHER : Wei_2014_Adv.Appl.Microbiol_89_267 |
PubMedSearch : Wei_2014_Adv.Appl.Microbiol_89_267 |
PubMedID: 25131405 |
Title : Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca - Roth_2014_Appl.Microbiol.Biotechnol_98_7815 |
Author(s) : Roth C , Wei R , Oeser T , Then J , Follner C , Zimmermann W , Strater N |
Ref : Applied Microbiology & Biotechnology , 98 :7815 , 2014 |
Abstract : Roth_2014_Appl.Microbiol.Biotechnol_98_7815 |
ESTHER : Roth_2014_Appl.Microbiol.Biotechnol_98_7815 |
PubMedSearch : Roth_2014_Appl.Microbiol.Biotechnol_98_7815 |
PubMedID: 24728714 |
Gene_locus related to this paper: thefu-q6a0i4 |
Title : Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch compost by using a metagenomic approach - Sulaiman_2012_Appl.Environ.Microbiol_78_1556 |
Author(s) : Sulaiman S , Yamato S , Kanaya E , Kim JJ , Koga Y , Takano K , Kanaya S |
Ref : Applied Environmental Microbiology , 78 :1556 , 2012 |
Abstract : Sulaiman_2012_Appl.Environ.Microbiol_78_1556 |
ESTHER : Sulaiman_2012_Appl.Environ.Microbiol_78_1556 |
PubMedSearch : Sulaiman_2012_Appl.Environ.Microbiol_78_1556 |
PubMedID: 22194294 |
Gene_locus related to this paper: 9bact-g9by57 |
Title : Crystal structure of cutinase Est119 from Thermobifida alba AHK119 that can degrade modified polyethylene terephthalate at 1.76A resolution - Kitadokoro_2012_Polym.Degrad.Stab_97_771 |
Author(s) : Kitadokoro K , Thumarat U , Nakamura R , Nishimura K , Karatani H , Suzuki H , Kawai F |
Ref : Polymer Degradation and Stability , 97 :771 , 2012 |
Abstract : Kitadokoro_2012_Polym.Degrad.Stab_97_771 |
ESTHER : Kitadokoro_2012_Polym.Degrad.Stab_97_771 |
PubMedSearch : Kitadokoro_2012_Polym.Degrad.Stab_97_771 |
PubMedID: |
Gene_locus related to this paper: 9acto-f7ix06 |
Title : Structure of a microbial homologue of mammalian platelet-activating factor acetylhydrolases: Streptomyces exfoliatus lipase at 1.9 A resolution - Wei_1998_Structure_6_511 |
Author(s) : Wei Y , Swenson L , Castro C , Derewenda U , Minor W , Arai H , Aoki J , Inoue K , Servin-Gonzalez L , Derewenda ZS |
Ref : Structure , 6 :511 , 1998 |
Abstract : Wei_1998_Structure_6_511 |
ESTHER : Wei_1998_Structure_6_511 |
PubMedSearch : Wei_1998_Structure_6_511 |
PubMedID: 9562561 |
Gene_locus related to this paper: strex-lipas |
Title : Structure and function engineered Pseudomonas mendocina lipase - |
Author(s) : Boston M , Requadt C , Danko S , Jarnagin A , Ashizawa E , Wu S , Poulose AJ , Bott R |
Ref : Methods Enzymol , 284 :298 , 1997 |
PubMedID: 9379942 |
Gene_locus related to this paper: pseme-LIPA , psemy-a4y035 |