Literature summary for 3.1.1.101 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 .

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Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Organism	UniProt	Comment	Textmining
Ideonella sakaiensis	A0A0K8P6T7	-	-
Ideonella sakaiensis 201-F6	A0A0K8P6T7	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Ideonella sakaiensis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
(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	-	?
(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	-	?
4-nitrophenyl acetate + H2O	-	Ideonella sakaiensis	acetate + 4-nitrophenol	-	?
4-nitrophenyl acetate + H2O	-	Ideonella sakaiensis 201-F6	acetate + 4-nitrophenol	-	?

Synonyms

Synonyms	Comment	Organism
PETase	-	Ideonella sakaiensis