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1. Yoshida  S, Hiraga  K, Takehana  T, Taniguchi  I, Yamaji  H, Maeda  Y, Toyohara  K, Miyamoto  K, Kimura  Y, Oda  K,     ( 2016 )

A bacterium that degrades and assimilates poly(ethylene terephthalate).

Science (New York, N.Y.) 351 (6278)
PMID : 26965627  :   DOI  :   10.1126/science.aad6359     DOI  :   10.1126/science.aad6359    
Abstract >>
Poly(ethylene terephthalate) (PET) is used extensively worldwide in plastic products, and its accumulation in the environment has become a global concern. Because the ability to enzymatically degrade PET has been thought to be limited to a few fungal species, biodegradation is not yet a viable remediation or recycling strategy. By screening natural microbial communities exposed to PET in the environment, we isolated a novel bacterium, Ideonella sakaiensis 201-F6, that is able to use PET as its major energy and carbon source. When grown on PET, this strain produces two enzymes capable of hydrolyzing PET and the reaction intermediate, mono(2-hydroxyethyl) terephthalic acid. Both enzymes are required to enzymatically convert PET efficiently into its two environmentally benign monomers, terephthalic acid and ethylene glycol.
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2. Han  X, Liu  W, Huang  JW, Ma  J, Zheng  Y, Ko  TP, Xu  L, Cheng  YS, Chen  CC, Guo  RT,     ( 2017 )

Structural insight into catalytic mechanism of PET hydrolase.

Nature communications 8 (1)
PMID : 29235460  :   DOI  :   10.1038/s41467-017-02255-z     PMC  :   PMC5727383    
Abstract >>
PET hydrolase (PETase), which hydrolyzes polyethylene terephthalate (PET) into soluble building blocks, provides an attractive avenue for the bioconversion of plastics. Here we present the structures of a novel PETase from the PET-consuming microbe Ideonella sakaiensis in complex with substrate and product analogs. Through structural analyses, mutagenesis, and activity measurements, a substrate-binding mode is proposed, and several features critical for catalysis are elucidated.
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3. Liu  B, He  L, Wang  L, Li  T, Li  C, Liu  H, Luo  Y, Bao  R,     ( 2018 )

Protein Crystallography and Site-Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis.

Chembiochem : a European journal of chemical biology N/A (N/A)
PMID : 29603535  :   DOI  :   10.1002/cbic.201800097    
Abstract >>
Unlike traditional recycling strategies, biodegradation is a sustainable solution for disposing of poly(ethylene terephthalate) (PET) waste. PETase, a newly identified enzyme from Ideonella sakaiensis, has high efficiency and specificity towards PET and is, thus, a prominent candidate for PET degradation. On the basis of biochemical analysis, we propose that a wide substrate-binding pocket is critical for its excellent ability to hydrolyze crystallized PET. Structure-guided site-directed mutagenesis revealed an improvement in PETase catalytic efficiency, providing valuable insight into how the molecular engineering of PETase can optimize its application in biocatalysis.
KeywordMeSH Terms
protein engineering
sustainable chemistry
waste disposal
4. Joo  S, Cho  IJ, Seo  H, Son  HF, Sagong  HY, Shin  TJ, Choi  SY, Lee  SY, Kim  KJ,     ( 2018 )

Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation.

Nature communications 9 (1)
PMID : 29374183  :   DOI  :   10.1038/s41467-018-02881-1     PMC  :   PMC5785972    
Abstract >>
Plastics, including poly(ethylene terephthalate) (PET), possess many desirable characteristics and thus are widely used in daily life. However, non-biodegradability, once thought to be an advantage offered by plastics, is causing major environmental problem. Recently, a PET-degrading bacterium, Ideonella sakaiensis, was identified and suggested for possible use in degradation and/or recycling of PET. However, the molecular mechanism of PET degradation is not known. Here we report the crystal structure of I. sakaiensis PETase (IsPETase) at 1.5 ? resolution. IsPETase has a Ser-His-Asp catalytic triad at its active site and contains an optimal substrate binding site to accommodate four monohydroxyethyl terephthalate (MHET) 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. Moreover, other PETase candidates potentially having high PET-degrading activities are suggested based on phylogenetic tree analysis of 69 PETase-like proteins.
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5. 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,     ( 2018 )

Characterization and engineering of a plastic-degrading aromatic polyesterase.

Proceedings of the National Academy of Sciences of the United States of America 115 (19)
PMID : 29666242  :   DOI  :   10.1073/pnas.1718804115     PMC  :   PMC5948967    
Abstract >>
Poly(ethylene terephthalate) (PET) is one of the most abundantly produced synthetic polymers and is accumulating in the environment at a staggering rate as discarded packaging and textiles. The properties that make PET so useful also endow it with an alarming resistance to biodegradation, likely lasting centuries in the environment. Our collective reliance on PET and other plastics means that this buildup will continue unless solutions are found. Recently, a newly discovered bacterium, Ideonella sakaiensis 201-F6, was shown to exhibit the rare ability to grow on PET as a major carbon and energy source. Central to its PET biodegradation capability is a secreted PETase (PET-digesting enzyme). Here, we present a 0.92 ? resolution X-ray crystal structure of PETase, which reveals features common to both cutinases and lipases. PETase retains the ancestral �\/�]-hydrolase fold but exhibits a more open active-site cleft than homologous cutinases. By narrowing the binding cleft via mutation of two active-site residues to conserved amino acids in cutinases, we surprisingly observe improved PET degradation, suggesting that PETase is not fully optimized for crystalline PET degradation, despite presumably evolving in a PET-rich environment. Additionally, we show that PETase degrades another semiaromatic polyester, polyethylene-2,5-furandicarboxylate (PEF), which is an emerging, bioderived PET replacement with improved barrier properties. In contrast, PETase does not degrade aliphatic polyesters, suggesting that it is generally an aromatic polyesterase. These findings suggest that additional protein engineering to increase PETase performance is realistic and highlight the need for further developments of structure/activity relationships for biodegradation of synthetic polyesters.
KeywordMeSH Terms
plastics recycling
poly(ethylene furanoate)
poly(ethylene terephthalate)
6. Fecker  T, Galaz-Davison  P, Engelberger  F, Narui  Y, Sotomayor  M, Parra  LP, Ramírez-Sarmiento  CA,     ( 2018 )

Active Site Flexibility as a Hallmark for Efficient PET Degradation by I. sakaiensis PETase.

Biophysical journal 114 (6)
PMID : 29590588  :   DOI  :   10.1016/j.bpj.2018.02.005     PMC  :   PMC5883944    
Abstract >>
Polyethylene terephthalate (PET) is one of the most-consumed synthetic polymers, with an annual production of 50 million tons. Unfortunately, PET accumulates as waste and is highly resistant to biodegradation. Recently, fungal and bacterial thermophilic hydrolases were found to catalyze PET hydrolysis with optimal activities at high temperatures. Strikingly, an enzyme from Ideonella sakaiensis, termed PETase, was described to efficiently degrade PET at room temperature, but the molecular basis of its activity is not currently understood. Here, a crystal structure of PETase was determined at 2.02 ? 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. Molecular docking of a model substrate predicts that PET binds to PETase in a unique and energetically favorable conformation facilitated by several residue substitutions within its active site when compared to other enzymes. These computational predictions are in excellent agreement with recent mutagenesis and PET film degradation analyses. Finally, we rationalize the increased catalytic activity of PETase at room temperature through molecular dynamics simulations of enzyme-ligand complexes for PETase and other thermophilic PET-degrading enzymes at 298, 323, and 353 K. Our results reveal that both the binding pose and residue substitutions within PETase favor proximity between the catalytic residues and the labile carbonyl of the substrate at room temperature, suggesting a more favorable hydrolytic reaction. These results are valuable for enabling detailed evolutionary analysis of PET-degrading enzymes and for rational design endeavors aiming at increasing the efficiency of PETase and similar enzymes toward plastic degradation.
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Catalytic Domain

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