Literature summary for 3.1.1.74 extracted from

Araujo, R.; Silva, C.; ONeill, A.; Micaelo, N.; Guebitz, G.; Soares, C.M.; Casal, M.; Cavaco-Paulo, A.
Tailoring cutinase activity towards polyethylene terephthalate and polyamide 6,6 fibers (2007), J. Biotechnol., 128, 849-857.

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Protein Variants

Protein Variants	Comment	Organism
L182A	shows the one- and two-fold higher ability to biodegrade aliphatic polyamide substrates. Activity with polyethylene terephthalate fibers is 5.3fold higher than wild-type enzyme, activity with polyamide 6,6 fiber is 119% of wild-type activity	Fusarium solani
L189A	activity with polyethylene terephthalate fibers is 78% of wild-type enzyme, activity with polyamide 6,6 fiber is 94% of wild-type activity	Fusarium solani
L81A	activity with polyethylene terephthalate fibers is 4fold higher than wild-type enzyme, activity with polyamide 6,6 fiber is 98% of wild-type activity	Fusarium solani
N84A	activity with polyethylene terephthalate fibers is 1.7fold higher than wild-type enzyme, activity with polyamide 6,6 fiber is 93% of wild-type activity	Fusarium solani
V184A	activity with polyethylene terephthalate fibers is 2fold higher than wild-type enzyme, activity with polyamide 6,6 fiber is 98% of wild-type activity	Fusarium solani

Organism

Organism	UniProt	Comment	Textmining
Fusarium solani	P00590	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
polyamide + H2O	-	Fusarium solani	?	-	?
polyethylene terephthalate + H2O	-	Fusarium solani	terephthalate + ?	-	?

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Release 2023.1 (January 2023)