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Literature summary for 4.1.2.48 extracted from

  • di Salvo, M.L.; Remesh, S.G.; Vivoli, M.; Ghatge, M.S.; Paiardini, A.; D'Aguanno, S.; Safo, M.K.; 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
Search for more literature for 4.1.2.48

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
at 2.2 A resolution, in the unliganded form and cocrystallized with L-serine and L-threonine. No active site catalytic residue is revealed, and a structural water molecule is assumed to act as the catalytic base in the retro-aldol cleavage reaction. The very large active site opening suggests that much larger molecules than L-threonine isomers may be easily accommodated Escherichia coli

Protein Variants

Protein Variants Comment Organism
F87A no change in the ration of cleavage of L-threonine to L-allo-threonine Escherichia coli
F87D mutation doubles the preference of the enzyme for L-allo-threonine Escherichia coli
H126F 300% of wild-type activity,reduced preference for the erythro-substrate Escherichia coli
H126N 60% of wild-type activity Escherichia coli
H83F less than 1% of wild-type activity, reduced preference for the erythro-substrate Escherichia coli
H83F/H126F able to catalyze the cleavage of both L-threonine and L-allo-threonine at a measurable rate, neither of the histidines acts as a catalytic base in the retro-aldol cleavage mechanism Escherichia coli
H83N less than 10% of wild-type activity Escherichia coli
K222A slight decrease in kcat and slight increase in Km values for both L-threonine and L-allo-threonine Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
 L-allo-threonine mutant H126NF, pH 7.0, 30°C Escherichia coli
0.24
-
 L-allo-threonine wild-type, pH 7.0, 30°C Escherichia coli
0.4
-
 L-threonine mutant F87A, pH 7.0, 30°C Escherichia coli
0.96
-
 L-allo-threonine mutant H126N, pH 7.0, 30°C Escherichia coli
1.1
-
 L-threonine mutant H83F/H126F, pH 7.0, 30°C Escherichia coli
1.3
-
 L-allo-threonine mutant F87A, pH 7.0, 30°C Escherichia coli
1.3
-
 L-threonine mutant F87D, pH 7.0, 30°C Escherichia coli
1.7
-
 L-allo-threonine mutant F87D, pH 7.0, 30°C Escherichia coli
1.7
-
 L-threonine mutant H126F, pH 7.0, 30°C Escherichia coli
1.7
-
 L-allo-threonine mutant H83N, pH 7.0, 30°C Escherichia coli
3.7
-
 L-threonine mutant K222A, pH 7.0, 30°C Escherichia coli
5
-
 L-allo-threonine mutant K222A, pH 7.0, 30°C Escherichia coli
7
-
 L-threonine mutant H83F, pH 7.0, 30°C Escherichia coli
7
-
 L-allo-threonine mutant H83F, pH 7.0, 30°C Escherichia coli
19.4
-
 L-threonine wild-type, pH 7.0, 30°C Escherichia coli
31
-
 L-allo-threonine mutant H83F/H126F, pH 7.0, 30°C Escherichia coli
38
-
 L-threonine mutant H83N, pH 7.0, 30°C Escherichia coli
61
-
 L-threonine mutant H126N, pH 7.0, 30°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli WV_060327
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-allo-threonine
-
 Escherichia coli glycine + acetaldehyde
-
 ?
L-allo-threonine
-
 Escherichia coli WV_060327 glycine + acetaldehyde
-
 ?
L-threonine
-
 Escherichia coli glycine + acetaldehyde
-
 ?
L-threonine
-
 Escherichia coli WV_060327 glycine + acetaldehyde
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.02
-
 L-threonine mutant H83F, pH 7.0, 30°C Escherichia coli
0.06
-
 L-allo-threonine mutant H83F, pH 7.0, 30°C Escherichia coli
0.28
-
 L-threonine mutant H83N, pH 7.0, 30°C Escherichia coli
1.28
-
 L-allo-threonine mutant H83N, pH 7.0, 30°C Escherichia coli
1.87
-
 L-threonine wild-type, pH 7.0, 30°C Escherichia coli
3.55
-
 L-allo-threonine wild-type, pH 7.0, 30°C Escherichia coli
4.37
-
 L-threonine mutant H126N, pH 7.0, 30°C Escherichia coli
6
-
 L-threonine mutant H126F, pH 7.0, 30°C Escherichia coli
7.82
-
 L-allo-threonine mutant H126N, pH 7.0, 30°C Escherichia coli
9.02
-
 L-allo-threonine mutant H126NF, pH 7.0, 30°C Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.01
-
 L-allo-threonine mutant H83F, pH 7.0, 30°C Escherichia coli
0.01
-
 L-threonine mutant H83N, pH 7.0, 30°C Escherichia coli
0.07
-
 L-threonine mutant H126N, pH 7.0, 30°C Escherichia coli
0.1
-
 L-threonine wild-type, pH 7.0, 30°C Escherichia coli
0.75
-
 L-allo-threonine mutant H83N, pH 7.0, 30°C Escherichia coli
3.53
-
 L-threonine mutant H126F, pH 7.0, 30°C Escherichia coli
8.13
-
 L-allo-threonine mutant H126N, pH 7.0, 30°C Escherichia coli
14.78
-
 L-allo-threonine wild-type, pH 7.0, 30°C Escherichia coli
45.08
-
 L-allo-threonine mutant H126NF, pH 7.0, 30°C Escherichia coli