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Literature summary for 1.4.1.20 extracted from

  • Paradisi, F.; Collins, S.; Maguire, A.R.; Engel, P.C.
    Phenylalanine dehydrogenase mutants: Efficient biocatalysts for synthesis of non-natural phenylalanine derivatives (2007), J. Biotechnol., 128, 408-411.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
N145A 4-trifluoromethyl-phenylpyruvate is the preferred substrate, the reaction velocity at elevated substrate concentration (5 mM) is almost 10 times higher compared to the wild type enzyme Lysinibacillus sphaericus
N145L 4-methoxy-phenylpyruvate is the preferred substrate Lysinibacillus sphaericus
N145V 4-fluoro-phenylpyruvate is the preferred substrate Lysinibacillus sphaericus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.45
-
4-trifluoromethyl-phenylpyruvate mutant enzyme N145A, at 25°C inTris buffer 50mM pH 8.5, with NADH (0.1 mM), KCl (100 mM) and NH4Cl (400 mM) Lysinibacillus sphaericus

Organism

Organism UniProt Comment Textmining
Lysinibacillus sphaericus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-fluoro-phenylpyruvate + NH3 + NADH preferred substrate of mutant N145V Lysinibacillus sphaericus 4-fluoro-L-phenylalanine + H2O + NAD+
-
r
4-methoxy-phenylpyruvate + NH3 + NADH preferred substrate of mutant N145L Lysinibacillus sphaericus 4-methoxy-L-phenylalanine + H2O + NAD+
-
r
4-trifluoromethyl-phenylpyruvate + NH3 + NADH preferred substrate of mutant N145A Lysinibacillus sphaericus 4-trifluoromethyl-L-phenylalanine + H2O + NAD+
-
r

Synonyms

Synonyms Comment Organism
PheDH
-
Lysinibacillus sphaericus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Lysinibacillus sphaericus