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Literature summary for 4.1.2.48 extracted from

  • Di Salvo, M.; Remesh, S.; Vivoli, M.; Ghatge, M.; Paiardini, A.; DAguanno, S.; Safo, M.; Contestabile, R.
    On the catalytic mechanism and stereospecificity of Escherichia coli L-threonine aldolase (2014), FEBS J., 281, 129-145 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
synthesis the enzyme may be exploited for bioorganic synthesis of L-3-hydroxyamino acids that are biologically active or constitute building blocks for pharmaceutical molecules Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structure of the low-specificity L-threonine aldolase is determined at 2.2 A resolution, in the unliganded form and co-crystallized with L-serine and L-threonine Escherichia coli

Protein Variants

Protein Variants Comment Organism
F87A catalytic efficiency of the mutant enzyme for L-threonine is 1.7fold lower than that of the wild-type enzyme, catalytic efficiency of the mutant enzyme for L-allo-threonine is 1.2fold lower than that of the wild-type enzyme Escherichia coli
F87D catalytic efficiency of the mutant enzyme for L-threonine is 3.11fold lower than that of the wild-type enzyme, catalytic efficiency of the mutant enzyme for L-allo-threonine is 7.5fold lower than that of the wild-type enzyme Escherichia coli
H83F/H126F catalytic efficiency of the mutant enzyme for L-threonine is 3890fold lower than that of the wild-type enzyme, catalytic efficiency of the mutant enzyme for L-allo-threonine is 294fold lower than that of the wild-type enzyme Escherichia coli
K222A catalytic efficiency of the mutant enzyme for L-threonine is 13.4fold lower than that of the wild-type enzyme, catalytic efficiency of the mutant enzyme for L-allo-threonine is 9.7fold lower than that of the wild-type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.24
-
L-allo-threonine pH 7.0, 30°C, wild-type enzyme Escherichia coli
0.31
-
L-allo-threonine pH 7.0, 30°C, mutant enzyme F87A Escherichia coli
0.41
-
L-allo-threonine pH 7.0, 30°C, mutant enzyme F87D Escherichia coli
1.2
-
L-allo-threonine pH 7.0, 30°C, mutant enzyme K222A Escherichia coli
7.4
-
L-allo-threonine pH 7.0, 30°C, mutant enzyme H83F/H126F Escherichia coli
8.7
-
L-threonine pH 7.0, 30°C, mutant enzyme F87A Escherichia coli
19.4
-
L-threonine pH 7.0, 30°C, wild-type enzyme Escherichia coli
21
-
L-threonine pH 7.0, 30°C, mutant enzyme H83F/H126F Escherichia coli
24.9
-
L-threonine pH 7.0, 30°C, mutant enzyme F87D Escherichia coli
72
-
L-threonine pH 7.0, 30°C, mutant enzyme K222A Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P75823
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-allo-threonine
-
Escherichia coli glycine + acetaldehyde
-
?
L-threonine
-
Escherichia coli glycine + acetaldehyde
-
?

Synonyms

Synonyms Comment Organism
Low-specificity L-threonine aldolase
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0073
-
L-threonine pH 7.0, 30°C, mutant enzyme H83F/H126F Escherichia coli
0.028
-
L-allo-threonine pH 7.0, 30°C, mutant enzyme H83F/H126F Escherichia coli
0.33
-
L-threonine pH 7.0, 30°C, mutant enzyme F87D Escherichia coli
0.72
-
L-threonine pH 7.0, 30°C, mutant enzyme F87A Escherichia coli
0.72
-
L-threonine pH 7.0, 30°C, mutant enzyme K222A Escherichia coli
1.33
-
L-allo-threonine pH 7.0, 30°C, mutant enzyme K222A Escherichia coli
1.87
-
L-threonine pH 7.0, 30°C, wild-type enzyme Escherichia coli
1.95
-
L-allo-threonine pH 7.0, 30°C, mutant enzyme F87D Escherichia coli
2.7
-
L-allo-threonine pH 7.0, 30°C, mutant enzyme F87A Escherichia coli
3.55
-
L-allo-threonine pH 7.0, 30°C, wild-type enzyme Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.00033
-
L-allo-threonine pH 7.0, 30°C, mutant enzyme H83F/H126F Escherichia coli
0.0038
-
L-threonine pH 7.0, 30°C, mutant enzyme H83F/H126F Escherichia coli
0.01
-
L-allo-threonine pH 7.0, 30°C, mutant enzyme K222A Escherichia coli
0.013
-
L-allo-threonine pH 7.0, 30°C, mutant enzyme F87D Escherichia coli
0.082
-
L-allo-threonine pH 7.0, 30°C, mutant enzyme F87A Escherichia coli
0.097
-
L-allo-threonine pH 7.0, 30°C, wild-type enzyme Escherichia coli
1.1
-
L-threonine pH 7.0, 30°C, mutant enzyme K222A Escherichia coli
4.75
-
L-threonine pH 7.0, 30°C, mutant enzyme F87D Escherichia coli
8.6
-
L-threonine pH 7.0, 30°C, mutant enzyme F87A Escherichia coli
14.78
-
L-threonine pH 7.0, 30°C, wild-type enzyme Escherichia coli