Literature summary for 1.3.1.12 extracted from

Christendat, D.; Saridakis, V.C.; Turnbull, J.L.
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli (1998), Biochemistry, 37, 15703-15712.

Search for more literature for 1.3.1.12

Cloned(Commentary)

Cloned (Comment)	Organism
T7 expression system	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
H131A	chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme retains 10% of dehydrogenase activity and 30% mutase activity compared to the wild-type enzyme, His131 is not an essential residue whose protonation state is critical for catalysis or substrate binding	Escherichia coli
H189N	chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme shows less than 0.01% the activity of wild-type mutase and dehydrogenase	Escherichia coli
H197N	chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme exhibits no significant dehydrogenase activity, retains nearly wild-type mutase activity and unaltered Michaelis constants for chorismate, prephenate and NAD+	Escherichia coli
K37A	chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant protein poorly expressed, no detectable mutase or dehydrogenase activity, structural changes may result in its inactivity and instability	Escherichia coli
K37Q	chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme exhibits no mutase activity while retaining wild-type dehydrogenase activity	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.045	0.09	prephenate	-	Escherichia coli
0.054	0.055	prephenate	mutant forms K37Q and H197N	Escherichia coli
0.103	-	NAD+	wild-type enzyme	Escherichia coli
0.128	0.141	NAD+	mutant forms H197N and K37Q	Escherichia coli

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	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
chorismate mutase-prephenate dehydrogenase bifunctional enzyme	Escherichia coli
wild-type and mutant enzyme	Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	-	Escherichia coli

Storage Stability

Storage Stability	Organism
4°C, ammonium sulfate precipitate	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
prephenate + NAD+	-	Escherichia coli	4-hydroxyphenylpyruvate + NADH + CO2	-	?
prephenate + NAD+	biosynthesis of L-tyrosine	Escherichia coli	4-hydroxyphenylpyruvate + NADH + CO2	-	?

Synonyms

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

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.00005	-	prephenate	mutant enzyme H197N	Escherichia coli
0.0000583	-	NAD+	mutant enzyme H197N	Escherichia coli
0.367	-	NAD+	mutant enzyme K37Q	Escherichia coli
0.383	-	prephenate	mutant enzyme K37Q	Escherichia coli
0.45	-	NAD+	wild-type enzyme	Escherichia coli
0.45	-	prephenate	wild-type enzyme	Escherichia coli

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Release 2023.1 (January 2023)