Literature summary for 4.3.1.24 extracted from

Sarkissian, C.N.; Gamez, A.; Wang, L.; Charbonneau, M.; Fitzpatrick, P.; Lemontt, J.F.; Zhao, B.; Vellard, M.; Bell, S.M.; Henschell, C.; Lambert, A.; Tsuruda, L.; Stevens, R.C.; Scriver, C.R.
Preclinical evaluation of multiple species of PEGylated recombinant phenylalanine ammonia lyase for the treatment of phenylketonuria (2008), Proc. Natl. Acad. Sci. USA, 105, 20894-20899.

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Protein Variants

Protein Variants	Comment	Organism
C503S/C565S	the mutant shows high protein stability and is very efficient as protein therapeutics in treatment of phenylketonuria, PKU, with lowered phenylalanine levels in both vascular space and brain tissue over a 90 day trial period, resulting in reduced manifestations associated with PKU, including reversal of PKU-associated hypopigmentation and enhanced animal health in a mouse model, the wild-type enzyme is less efective, overview	Trichormus variabilis
R91K	the mutant shows increased activity compared to the wild-type enzyme	Trichormus variabilis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-phenylalanine	Trichormus variabilis	-	(E)-cinnamate + NH3	-	?

Organism

Organism	UniProt	Comment	Textmining
Trichormus variabilis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-phenylalanine	-	Trichormus variabilis	(E)-cinnamate + NH3	-	?

Synonyms

Synonyms	Comment	Organism
PAL	-	Trichormus variabilis

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Release 2023.1 (January 2023)