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Literature summary extracted from

  • Fecker, T.; Galaz-Davison, P.; Engelberger, F.; Narui, Y.; Sotomayor, M.; Parra, L.P.; Ramirez-Sarmiento, C.A.
    Active site flexibility as a hallmark for efficient PET degradation by I. sakaiensis PETase (2018), Biophys. J., 114, 1302-1312 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.101 cloned into a pET24b vector and transformed into Escherichia coli BL21-Gold(DE3) Ideonella sakaiensis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.101 sitting drop vapor diffusion method at 4°C with a mixture at a 1:1 ratio of protein and reservoir solution. Crystal structure of PETase is determined at 2.02 A 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. High flexibility of PETase loops at room temperature enables this enzyme to bind and degrade PET more efficiently than other cutinases Ideonella sakaiensis

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.101 Ideonella sakaiensis A0A0K8P6T7
-
-
3.1.1.101 Ideonella sakaiensis 201-F6 A0A0K8P6T7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.101
-
 Ideonella sakaiensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.101 (ethylene terephthalate)n + H2O high flexibility of PETase loops at room temperature enables this enzyme to bind and degrade PET more efficiently than other cutinases Ideonella sakaiensis (ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
 ?
3.1.1.101 (ethylene terephthalate)n + H2O high flexibility of PETase loops at room temperature enables this enzyme to bind and degrade PET more efficiently than other cutinases Ideonella sakaiensis 201-F6 (ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
 ?
3.1.1.101 4-nitrophenyl acetate + H2O
-
 Ideonella sakaiensis acetate + 4-nitrophenol
-
 ?
3.1.1.101 4-nitrophenyl acetate + H2O
-
 Ideonella sakaiensis 201-F6 acetate + 4-nitrophenol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.101 PETase
-
 Ideonella sakaiensis