Literature summary for 3.1.1.101 extracted from

Austin, H.P.; Allen, M.D.; Donohoe, B.S.; Rorrer, N.A.; Kearns, F.L.; Silveira, R.L.; Pollard, B.C.; Dominick, G.; Duman, R.; El Omari, K.; Mykhaylyk, V.; Wagner, A.; Michener, W.E.; Amore, A.; Skaf, M.S.; Crowley, M.F.; Thorne, A.W.; Johnson, C.W.; Woodcock, H.L.; McGeehan, J.E.; Beckham, G.T.
Characterization and engineering of a plastic-degrading aromatic polyesterase (2018), Proc. Natl. Acad. Sci. USA, 115, E4350-E4357 .

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Application

Application	Comment	Organism
environmental protection	the investigation of structure/function relationships can be used to guide further protein engineering to more effectively depolymerize PET and other synthetic polymers, thus informing a biotechnological strategy to help remediate the environmental scourge of plastic accumulation in nature	Ideonella sakaiensis

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Ideonella sakaiensis

Crystallization (Commentary)

Crystallization (Comment)	Organism
0.92 A resolution X-ray crystal structure reveals features common to both cutinases and lipases. PETase retains the ancestral alpha/beta-hydrolase fold but exhibits a more open active-site cleft than homologous cutinases	Ideonella sakaiensis

Protein Variants

Protein Variants	Comment	Organism
S238F/W159H	the mutant enzyme adopts a more productive interaction with PET	Ideonella sakaiensis

Organism

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(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	-	?
polyethylene-2,5-furandicarboxylate + H2O	-	Ideonella sakaiensis	?	-	?
polyethylene-2,5-furandicarboxylate + H2O	-	Ideonella sakaiensis 201-F6	?	-	?

Synonyms

Synonyms	Comment	Organism
PETase	-	Ideonella sakaiensis

pI Value

Organism	Comment	pI Value Maximum	pI Value
Ideonella sakaiensis	-	-	9.6

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Release 2023.1 (January 2023)