Literature summary for 1.4.1.20 extracted from

Seah, S.Y.; Britton, K.L.; Baker, P.J.; Rice, D.W.; Asano, Y.; Engel, P.C.
Alteration in relative activities of phenylalanine dehydrogenase towards different substrates by site-directed mutagenesis (1995), FEBS Lett., 370, 93-96.

Search for more literature for 1.4.1.20

Cloned(Commentary)

Cloned (Comment)	Organism
wild-type and mutant enzymes L307V, G124A and G124A/L307V expressed in Escherichia coli	Lysinibacillus sphaericus

Protein Variants

Protein Variants	Comment	Organism
G124A	mutant enzyme has lower activity towards L-Phe and enhanced activity towards almost all aliphatic amino acid substrates compared to the wild-type	Lysinibacillus sphaericus
G124A/L307V	mutant enzyme has lower activity towards L-Phe and enhanced activity towards almost all aliphatic amino acid substrates compared to the wild-type	Lysinibacillus sphaericus
L307V	mutant enzyme has lower activity towards L-Phe and enhanced activity towards almost all aliphatic amino acid substrates compared to the wild-type	Lysinibacillus sphaericus

Organism

Organism	UniProt	Comment	Textmining
Lysinibacillus sphaericus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-Phe + H2O + NAD+	-	Lysinibacillus sphaericus	phenylpyruvate + NH3 + NADH	-	r

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Lysinibacillus sphaericus
NADH	-	Lysinibacillus sphaericus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)