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Literature summary extracted from

  • Hou, Y.; Hossain, G.; Li, J.; Shin, H.D.; Du, G.; Liu, L.
    Combination of phenylpyruvic acid (PPA) pathway engineering and molecular engineering of L-amino acid deaminase improves PPA production with an Escherichia coli whole-cell biocatalyst (2016), Appl. Microbiol. Biotechnol., 100, 2183-2191.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.4.3.2 synthesis engineering Escherichia coli to produce phenylpyruvate. Knock-out of three aminotransferases increases the phenylpyuvate titer from 3.3 to 3.9 g/l and the substrate conversion ratio to 97.5%. The L-amino acid deaminase triple mutant D165K/F263M/L336M produces 10.0 g phenylpyruvate per l, with a substrate conversion ratio of 100%. An optimal fed-batch biotransformation process gives 21 g phenylpyruvate per l within 8 h Proteus mirabilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.3.2 xcpression in Escherichia coli Proteus mirabilis

Protein Variants

EC Number Protein Variants Comment Organism
1.4.3.2 D165K slight increase in kcat/KM value for phenylpyruvate Proteus mirabilis
1.4.3.2 D165K/F263M slight increase in kcat/KM value for phenylpyruvate Proteus mirabilis
1.4.3.2 D165K/F263M/L336 2fold increase in kcat/KM value for phenylpyruvate Proteus mirabilis
1.4.3.2 D165K/L336M slight increase in kcat/KM value for phenylpyruvate Proteus mirabilis
1.4.3.2 D165K/S179L/F263V/L336V slight increase in kcat/KM value for phenylpyruvate Proteus mirabilis
1.4.3.2 F263M slight increase in kcat/KM value for phenylpyruvate Proteus mirabilis
1.4.3.2 F263M/L336M 2fold increase in kcat/KM value for phenylpyruvate Proteus mirabilis
1.4.3.2 L336M slight increase in kcat/KM value for phenylpyruvate Proteus mirabilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.2 22
-
 L-phenylalanine mutant D165K/F263M/L336M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 22.4
-
 L-phenylalanine mutant F263M/L336M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 22.6
-
 L-phenylalanine mutant D165K/F263M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 23.8
-
 L-phenylalanine mutant F263M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 24.1
-
 L-phenylalanine mutant D165K/S179L/F263V/L336V, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 24.3
-
 L-phenylalanine mutant D165K/L336M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 24.5
-
 L-phenylalanine mutant L336M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 24.8
-
 L-phenylalanine mutant D165K, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 26.2
-
 L-phenylalanine wild-type, pH 7.0, temperature not specified in the publication Proteus mirabilis

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.2 Proteus mirabilis
-
-
-
1.4.3.2 Proteus mirabilis KCTC 2566
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.2 L-phenylalanine + H2O + O2
-
 Proteus mirabilis phenylpyruvate + NH3 + H2O2
-
 ?
1.4.3.2 L-phenylalanine + H2O + O2
-
 Proteus mirabilis KCTC 2566 phenylpyruvate + NH3 + H2O2
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.3.2 1.4
-
 L-phenylalanine wild-type, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 1.67
-
 L-phenylalanine mutant D165K, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 1.69
-
 L-phenylalanine mutant L336M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 1.72
-
 L-phenylalanine mutant D165K/L336M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 1.82
-
 L-phenylalanine mutant D165K/S179L/F263V/L336V, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 1.87
-
 L-phenylalanine mutant F263M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 2.16
-
 L-phenylalanine mutant D165K/F263M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 2.21
-
 L-phenylalanine mutant F263M/L336M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 2.25
-
 L-phenylalanine mutant D165K/F263M/L336M, pH 7.0, temperature not specified in the publication Proteus mirabilis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.4.3.2 0.053
-
 L-phenylalanine wild-type, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 0.067
-
 L-phenylalanine mutant D165K, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 0.069
-
 L-phenylalanine mutant L336M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 0.071
-
 L-phenylalanine mutant D165K/L336M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 0.076
-
 L-phenylalanine mutant D165K/S179L/F263V/L336V, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 0.079
-
 L-phenylalanine mutant F263M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 0.096
-
 L-phenylalanine mutant D165K/F263M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 0.099
-
 L-phenylalanine mutant F263M/L336M, pH 7.0, temperature not specified in the publication Proteus mirabilis
1.4.3.2 0.102
-
 L-phenylalanine mutant D165K/F263M/L336M, pH 7.0, temperature not specified in the publication Proteus mirabilis