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Literature summary extracted from

  • Kataoka, K.; Tanizawa, K.; Fukui, T.; Ueno, H.; Yoshimura, T.; Esaki, N.; Soda, K.
    Identification of active site lysyl residues of phenylalanine dehydrogenase by chemical modification with methyl acetyl phosphate combined with site-directed mutagenesis (1994), J. Biochem., 116, 1370-1376.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.4.1.20 K173A 37°C, t1/2 of the mutant enzyme is 60 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor Thermoactinomyces intermedius
1.4.1.20 K69A 37°C, t1/2 of the mutant enzyme is 50 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor. Km-value for L-Phe is 1400fold higher compared to wild type enzyme, Km-value for phenylpyruvate is 128fold higher compared to wild type enzyme. Turnover number for deamination is 686fold lower than that of wild-type enzyme, turnover-number for amination is 43fold lower than that of wild-type enzyme Thermoactinomyces intermedius
1.4.1.20 K69A/K81A 37°C, t1/2 of the mutant enzyme is 450 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor. Km-value for L-Phe is 200fold higher compared to wild type enzyme, Km-value for phenylpyruvate is 108fold higher compared to wild type enzyme. Turnover number for deamination is 110fold lower than that of wild-type enzyme, turnover-number for amination is 61fold lower than that of wild-type enzyme Thermoactinomyces intermedius
1.4.1.20 K81A 37°C, t1/2 of the mutant enzyme is 38 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor. Turnover number for deamination is 440fold lower than that of wild-type enzyme, turnover-number for amination is 42fold lower than that of wild-type enzyme Thermoactinomyces intermedius
1.4.1.20 K89A 37°C, t1/2 of the mutant enzyme is 75 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor Thermoactinomyces intermedius
1.4.1.20 K90A 37°C, t1/2 of the mutant enzyme is 80 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor Thermoactinomyces intermedius

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.20 methyl acetyl phosphate irreversible inactivation, simultaneous addition of substrate and coenzyme markedly protect from inactivation, the reagent can acetylate Lys69 and Lys81 Thermoactinomyces intermedius

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.20 0.017
-
 NADH mutant enzyme K69A/K81A Thermoactinomyces intermedius
1.4.1.20 0.026
-
 NADH mutant enzyme K81A Thermoactinomyces intermedius
1.4.1.20 0.051
-
 NADH mutant enzyme K69A Thermoactinomyces intermedius
1.4.1.20 0.052
-
 phenylpyruvate mutant enzyme K81A Thermoactinomyces intermedius
1.4.1.20 0.057
-
 NAD+ mutant enzyme K81A Thermoactinomyces intermedius
1.4.1.20 0.065
-
 phenylpyruvate wild-type enzyme Thermoactinomyces intermedius
1.4.1.20 0.081
-
 NAD+ mutant enzyme K69A/K81A Thermoactinomyces intermedius
1.4.1.20 0.083
-
 NADH wild-type enzyme Thermoactinomyces intermedius
1.4.1.20 0.09
-
 L-Phe mutant enzyme K81A Thermoactinomyces intermedius
1.4.1.20 0.1
-
 L-Phe wild-type enzyme Thermoactinomyces intermedius
1.4.1.20 0.16
-
 NAD+ mutant enzyme K69A Thermoactinomyces intermedius
1.4.1.20 0.17
-
 NAD+ wild-type enzyme Thermoactinomyces intermedius
1.4.1.20 7
-
 phenylpyruvate mutant enzyme K69A/K81A Thermoactinomyces intermedius
1.4.1.20 8.3
-
 phenylpyruvate mutant enzyme K69A Thermoactinomyces intermedius
1.4.1.20 20
-
 L-Phe mutant enzyme K69A/K81A Thermoactinomyces intermedius
1.4.1.20 140
-
 L-Phe mutant enzyme K69A Thermoactinomyces intermedius

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.20 Thermoactinomyces intermedius
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.20 L-Phe + H2O + NAD+
-
 Thermoactinomyces intermedius phenylpyruvate + NH3 + NADH
-
 r

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.4.1.20 37
-
 t1/2: 48 min, in absence of substrate or coenzyme. t1/2: 2000 min, in presence of 10 mM L-Leu and 1.0 mM NAD+ Thermoactinomyces intermedius

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.1.20 additional information
-
 additional information turnover numbers of wild-type and mutant enzymes Thermoactinomyces intermedius

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.20 NAD+
-
 Thermoactinomyces intermedius
1.4.1.20 NADH
-
 Thermoactinomyces intermedius