MHETase | |||||||||
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Identifiers | |||||||||
EC no. | 3.1.1.102 | ||||||||
Alt. names | MHET hydrolase, monohydroxyethyl terephthalate hydrolase | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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The enzyme MHETase is a hydrolase, which was discovered in 2016. It cleaves 2-hydroxyethyl terephthalic acid, the PET degradation product by PETase, to ethylene glycol and terephthalic acid. [1] This pair of enzymes, PETase and MHETase, enable the bacterium Ideonella sakaiensis to live on the plastic PET as sole carbon source.
The first enzyme of the PET degradation pathway, PETase, cleaves this plastic into the intermediates MHET (Mono-(2-hydroxyethyl)terephthalic acid) and minor amounts BHET (Bis-(2-hydroxyethyl)terephthalic acid). MHETase hydrolyses the ester bond of MHET forming terephthalic acid and ethylene glycol.
Besides its natural substrate MHET the chromogenic substrate MpNPT, mono-p-nitrophenyl-terephthalate, is also hydrolyzed well. This can be used to measure the enzymatic activity and determine the kinetic parameters. Ferulate and gallate esters, substrates of the closest relatives in the tannase family, are not converted. p-Nitrophenyl ester of aliphatic monocarboxylic acids like the widely used esterase substrate p-nitrophenyl acetate are not hydrolyzed either.
The native enzyme is incapable of working on BHET, mono(2-hydroxyethyl)-isophthalate (MHEI), or mono(2-hydroxyethyl)-furanoate (MHEF). MHEI is a likely industrial PET degradation product due to the use of isophthalate comonomer. MHEF is a product of PEF degradation by PETase. Protein engineering research aims to overcome these barriers. [2]
The structure of MHETase was solved in 2019. [3] It shows the common fold of the alpha/beta hydrolase superfamily. According to the classification in the ESTHER database, MHETase belongs to the family of tannases within block X. [4] This family mainly contains tannases und feruloyl esterases. The enzyme consists of two domains: the hydrolase domain harbors the catalytic residues Ser225, His528 and Asp492; the lid domain contributes most of the residues of the substrate binding site.
Polyethylene terephthalate (or poly(ethylene terephthalate), PET, PETE, or the obsolete PETP or PET-P), is the most common thermoplastic polymer resin of the polyester family and is used in fibres for clothing, containers for liquids and foods, and thermoforming for manufacturing, and in combination with glass fibre for engineering resins.
Cellulase is any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides:
Hydrolase is a class of enzyme that commonly perform as biochemical catalysts that use water to break a chemical bond, which typically results in dividing a larger molecule into smaller molecules. Some common examples of hydrolase enzymes are esterases including lipases, phosphatases, glycosidases, peptidases, and nucleosidases.
Although PET is used in several applications,, as of 2022 only bottles are collected at a substantial scale. The main motivations have been either cost reduction or recycle content of retail goods. An increasing amount is recycled back into bottles, the rest goes into fibres, film, thermoformed packaging and strapping. After sorting, cleaning and grinding, 'bottle flake' is obtained, which is then processed by either:
Dimethyl terephthalate (DMT) is an organic compound with the formula C6H4(COOCH3)2. It is the diester formed from terephthalic acid and methanol. It is a white solid that melts to give a distillable colourless liquid.
Polyethylene naphthalate is a polyester derived from naphthalene-2,6-dicarboxylic acid and ethylene glycol. As such it is related to poly(ethylene terephthalate), but with superior barrier properties.
Deubiquitinating enzymes (DUBs), also known as deubiquitinating peptidases, deubiquitinating isopeptidases, deubiquitinases, ubiquitin proteases, ubiquitin hydrolases, ubiquitin isopeptidases, are a large group of proteases that cleave ubiquitin from proteins. Ubiquitin is attached to proteins in order to regulate the degradation of proteins via the proteasome and lysosome; coordinate the cellular localisation of proteins; activate and inactivate proteins; and modulate protein-protein interactions. DUBs can reverse these effects by cleaving the peptide or isopeptide bond between ubiquitin and its substrate protein. In humans there are nearly 100 DUB genes, which can be classified into two main classes: cysteine proteases and metalloproteases. The cysteine proteases comprise ubiquitin-specific proteases (USPs), ubiquitin C-terminal hydrolases (UCHs), Machado-Josephin domain proteases (MJDs) and ovarian tumour proteases (OTU). The metalloprotease group contains only the Jab1/Mov34/Mpr1 Pad1 N-terminal+ (MPN+) (JAMM) domain proteases.
Polyester is a category of polymers that contain the ester functional group in every repeat unit of their main chain. As a specific material, it most commonly refers to a type called polyethylene terephthalate (PET). Polyesters include naturally occurring chemicals, such as in plants and insects, as well as synthetics such as polybutyrate. Natural polyesters and a few synthetic ones are biodegradable, but most synthetic polyesters are not. Synthetic polyesters are used extensively in clothing.
Chlorophyllase is an essential enzyme in chlorophyll metabolism. It is a membrane proteins commonly known as chlase (EC 3.1.1.14, CLH) with systematic name chlorophyll chlorophyllidohydrolase. It catalyzes the reaction
Aryldialkylphosphatase is a metalloenzyme that hydrolyzes the triester linkage found in organophosphate insecticides:
The enzyme tannase (EC 3.1.1.20) catalyzes the following reaction:
Bis(2-Hydroxyethyl) terephthalate is an organic compound; it is the ester of ethylene glycol and terephthalic acid. Together with 2-hydroxyethyl terephthalic acid, bis(2-Hydroxyethyl) terephthalate is an intermediate in the production of poly(ethylene terephthalate).
The enzyme pyrethroid hydrolase (EC 3.1.1.88, pyrethroid-hydrolyzing carboxylesterase, pyrethroid-hydrolysing esterase, pyrethroid-hydrolyzing esterase, pyrethroid-selective esterase, pyrethroid-cleaving enzyme, permethrinase, PytH, EstP; systematic name pyrethroid-ester hydrolase) catalyses the reaction
Ideonella is a genus of bacteria in the family Comamonadaceae.
N-acylethanolamine acid amide hydrolase (NAAA) EC 3.5.1.- is a member of the choloylglycine hydrolase family, a subset of the N-terminal nucleophile hydrolase superfamily. NAAA has a molecular weight of 31 kDa. The activation and inhibition of its catalytic site is of medical interest as a potential treatment for obesity and chronic pain. While it was discovered within the last decade, its structural similarity to the more familiar acid ceramidase (AC) and functional similarity to fatty acid amide hydrolase (FAAH) allow it to be studied extensively.
Ideonella sakaiensis is a bacterium from the genus Ideonella and family Comamonadaceae capable of breaking down and consuming the plastic polyethylene terephthalate (PET) using it as both a carbon and energy source. The bacterium was originally isolated from a sediment sample taken outside of a plastic bottle recycling facility in Sakai City, Japan.
John McGeehan is a British research scientist and scientific lead of the World Plastics Summit. He was professor of structural biology and director of the Centre for Enzyme Innovation (CEI) at the University of Portsmouth until 2022 and led a research team on enzyme engineering.
PETases are an esterase class of enzymes that catalyze the breakdown (via hydrolysis) of polyethylene terephthalate (PET) plastic to monomeric mono-2-hydroxyethyl terephthalate (MHET). The idealized chemical reaction is:
2-Hydroxyethyl terephthalic acid is an organic compound with the formula HOC2H4O2CC6H4CO2H. It is the monoester of terephthalic acid and ethylene glycol. The compound is a precursor to poly(ethylene terephthalate) (PET), a polymer that is produced on a large scale industrially. 2-Hydroxyethyl terephthalic acid is a colorless solid that is soluble in water and polar organic solvents. Near neutral pH, 2-hydroxyethyl terephthalic acid converts to 2-hydroxyethyl terephthalate, HOC2H4O2CC6H4CO2−.
Plastic degradation in marine bacteria describes when certain pelagic bacteria break down polymers and use them as a primary source of carbon for energy. Polymers such as polyethylene(PE), polypropylene (PP), and polyethylene terephthalate (PET) are incredibly useful for their durability and relatively low cost of production, however it is their persistence and difficulty to be properly disposed of that is leading to pollution of the environment and disruption of natural processes. It is estimated that each year there are 9-14 million metric tons of plastic that are entering the ocean due to inefficient solutions for their disposal. The biochemical pathways that allow for certain microbes to break down these polymers into less harmful byproducts has been a topic of study to develop a suitable anti-pollutant.