Literature summary for 1.3.1.12 extracted from

Hermes, J.D.; Tipton, P.A.; Fisher, M.A.; O'Leary, M.H.; Morrison, J.F.; Cleland, W.W.
Mechanisms of enzymatic and acid-catalyzed decarboxylations of prephenate (1984), Biochemistry, 23, 6263-6275.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
prephenate + NAD+	Escherichia coli	biosynthesis of L-tyrosine	4-hydroxyphenylpyruvate + NADH + CO2	-	ir

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
prephenate + NAD+	mechanism, kinetic studies	Escherichia coli	4-hydroxyphenylpyruvate + NADH + CO2	-	ir
prephenate + NAD+	biosynthesis of L-tyrosine	Escherichia coli	4-hydroxyphenylpyruvate + NADH + CO2	-	ir

Synonyms

Synonyms	Comment	Organism
chorismate mutase-prephenate dehydrogenase bifunctional enzyme	complex with EC 5.4.99.5	Escherichia coli

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Release 2023.1 (January 2023)