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Gene_locus Report for: idesa-peth

Ideonella sakaiensis (strain 201-F6) Poly(ethylene terephthalate) hydrolase (plastic degradation), PETase IsPETase

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)


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
Database
No mutation
34 structures (e.g. : 5XFY, 5XFZ, 5XG0... more)
No kinetic





5 substrates (e.g. : BHET, HEMT, MHET... more)
2 inhibitors: MHET, Terephthalic-acid
2 Genbank : WP_054022242, GAP38373
1 UniProt : A0A0K8P6T7
>3 Structure links 31 more: 8CRU, 8D1D, 8GU4
1 UniProt : A0A0K8P6T7
1 Interpro : A0A0K8P6T7
1 Prodom : A0A0K8P6T7
1 Pfam : A0A0K8P6T7
1 PIRSF : A0A0K8P6T7
1 SUPERFAM : A0A0K8P6T7
Sequence
Graphical view for this peptide sequence: idesa-peth
Colored MSA for Polyesterase-lipase-cutinase (raw)
MNFPRASRLMQAAVLGGLMAVSAAATAQTNPYARGPNPTAASLEASAGPF
TVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVPGYTARQSSIKWWGPR
LASHGFVVITIDTNSTLDQPSSRSSQQMAALRQVASLNGTSSSPIYGKVD
TARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWDSSTNFSSVTVPTLI
FACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALI
GKKGVAWMKRFMDNDTRYSTFACENPNSTRVSDFRTANCS
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

MNFPRASRLMQAAVLGGLMAVSAAATAQTNPYARGPNPTAASLEASAGPF
TVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVPGYTARQSSIKWWGPR
LASHGFVVITIDTNSTLDQPSSRSSQQMAALRQVASLNGTSSSPIYGKVD
TARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWDSSTNFSSVTVPTLI
FACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALI
GKKGVAWMKRFMDNDTRYSTFACENPNSTRVSDFRTANCS


References
34 more
    Title: Ancestral Sequence Reconstruction Identifies Structural Changes Underlying the Evolution of Ideonella sakaiensis PETase and Variants with Improved Stability and Activity
    Joho Y, Vongsouthi V, Spence MA, Ton J, Gomez C, Tan LL, Kaczmarski JA, Caputo AT, Royan S and Ardevol A <1 more author(s)>
    Ref: Biochemistry, :, 2022 : PubMed

            

    Title: Machine learning-aided engineering of hydrolases for PET depolymerization
    Lu H, Diaz DJ, Czarnecki NJ, Zhu C, Kim W, Shroff R, Acosta DJ, Alexander BR, Cole HO and Alper HS <3 more author(s)>
    Ref: Nature, 604:662, 2022 : PubMed

            

    Title: Directed Evolution of an Efficient and Thermostable PET Depolymerase
    Bell E, Smithson R, Kilbride S, Foster J, Hardy F, Ramachandran S, Tedstone A, Haigh S, Garforth A and Green A <3 more author(s)>
    Ref: Chemrxiv, :, 2021 : PubMed

            


Other Papers


Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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