Polyesterase-lipase-cutinase

Relationship

Family: Polyesterase-lipase-cutinase

Block: L

Parent Family: No family

Comment

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

Database

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

Sequences

Peptide in Fasta
Nucleotide in Fasta
Alignment with Multalin Text only
Seed alignment with MAFFT No colour
Alignment with MAFFT No colour
Dendrogram The dnd file

Structures (147)

Genes Proteins in Polyesterase-lipase-cutinase family (191)

No fragment of genes

Structures in Polyesterase-lipase-cutinase family (147)

Substrates in Polyesterase-lipase-cutinase family (41)

Inhibitors in Polyesterase-lipase-cutinase family (7)

References (33)

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
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
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
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
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
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
PubMedID: 34492896
Gene_locus related to this paper: 9burk-a0a1w6l588

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
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
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
PubMedID: 33797026

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
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
PubMedID: 34075621
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
PubMedID:
Gene_locus related to this paper: 9burk-a0a1f4jxw8 , 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
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
PubMedID: 34044062
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
PubMedID: 33579411
Gene_locus related to this paper: idesa-mheth , idesa-peth

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
PubMedID: 34386313
Gene_locus related to this paper: sacvd-c7mve8

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
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
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
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
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
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
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
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
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
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
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
PubMedID: 25492421
Gene_locus related to this paper: sacvd-c7mve8

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
PubMedID: 24728714
Gene_locus related to this paper: thefu-q6a0i4

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
PubMedID: 25131405

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
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
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
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