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Literature summary for 4.3.1.19 extracted from

  • Chen, L.; Chen, Z.; Zheng, P.; Sun, J.; Zeng, A.P.
    Study and reengineering of the binding sites and allosteric regulation of biosynthetic threonine deaminase by isoleucine and valine in Escherichia coli (2013), Appl. Microbiol. Biotechnol., 97, 2939-2949.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Escherichia coli

Protein Variants

Protein Variants Comment Organism
E347F mutation decreases the K0.5 values of Thr without significant change of the n(H) value compared to wild-type. Mutant is strongly feedback-resistant to Ile compared to the wild-type enzyme. IC50 (Ile) is increased compared to wild-type Escherichia coli
E442A mutation increases the K0.5 value of Thr and n(H) value, comparing to those of the wild-type enzyme. IC50 (Ile) is decreased compared to wild-type Escherichia coli
F352A mutation decreases the K0.5 values of Thr without significant change of the n(H) value compared to wild-type. Mutant is strongly feedback-resistant to Ile compared to the wild-type enzyme. IC50 (Ile) is increased compared to wild-type Escherichia coli
F352A/I460F double mutant is more resistant to Ile inhibition than any single site mutant. Double mutations retains more than 85% activity even at 10 mM Ile Escherichia coli
F352A/R362F mutant shows both higher activity and stronger resistance to Ile inhibition compared to wild-type mice. Overexpression of mutant in Escherichia coli JW3591 significantly increases the production of ketobutyrate and Ile in comparison to the reference strains overexpressing wild-type Escherichia coli
G350E mutation increases the K0.5 value of Thr and n(H) value, comparing to those of the wild-type enzyme. IC50 (Ile) is decreased compared to wild-type Escherichia coli
G445E mutation G445E increased the K0.5 value of Thr without change of n(H) value compared to wild-type. IC50 (Ile) is slightly increased compared to wild-type Escherichia coli
I460F mutation decreases the K0.5 values of Thr without significant change of the n(H) value compared to wild-type. Mutant is strongly feedback-resistant to Ile compared to the wild-type enzyme. IC50 (Ile) is increased compared to wild-type Escherichia coli
I460F/R362F double mutant is more resistant to Ile inhibition than any single site mutant. Double mutations retains more than 85% activity even at 10 mM Ile Escherichia coli
R362F mutation decreases the K0.5 values of Thr without significant change of the n(H) value compared to wild-type. Mutant is strongly feedback-resistant to Ile compared to the wild-type enzyme. IC50 (Ile) is increased compared to wild-type Escherichia coli
Y369L mutant shows an 91fold increased IC50 (Ile) value compared to wild-type Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Ile inhibition of isoleucine can be reversed by valine Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Synonyms

Synonyms Comment Organism
Threonine deaminase
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Escherichia coli

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.009
-
pH 7.5, 30°C, mutant E442A Escherichia coli Ile
0.037
-
pH 7.5, 30°C, mutant G350E Escherichia coli Ile
0.067
-
pH 7.5, 30°C, wild-type Escherichia coli Ile
0.162
-
pH 7.5, 30°C, mutant G445E Escherichia coli Ile
2.32
-
pH 7.5, 30°C, mutant F352A Escherichia coli Ile
2.86
-
pH 7.5, 30°C, mutant E347F Escherichia coli Ile
3.27
-
pH 7.5, 30°C, mutant I460F Escherichia coli Ile
6.99
-
pH 7.5, 30°C, mutant R362F Escherichia coli Ile