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(R)-N-Cbz-alaninal + glycine
(2S,3R,4R)-2-amino-4-(benzyloxycarbonylamino)-3-hydroxypentanoic acid
(R)-N-Cbz-alaninal + glycine
(2S,3S,4R)-2-amino-4-(benzyloxycarbonylamino)-3-hydroxypentanoic acid
-
conversion: 40%, glycine concentration: 70 mM, reaction temperature: 4°C, yield: 30%, L-erythro/L-threo: 16:84
-
-
?
benzyloxyacetaldehyde + glycine
(2S,3R)-2-amino-4-(benzyloxy)-3-hydroxybutanoic acid
benzyloxyacetaldehyde + glycine
(2S,3S)-2-amino-4-(benzyloxy)-3-hydroxybutanoic acid
-
conversion: 45%, glycine concentration: 140 mM, reaction temperature: 25°C, yield: 30%, L-erythro/L-threo: 40:60
-
-
?
DL-erythro-phenylserine
glycine + benzaldehyde
-
-
-
?
DL-threo-(3-methylsulfonylphenyl)serine
glycine + 3-methylsulfonylbenzaldehyde
121% of the activity with L-threonine
-
-
?
DL-threo-(3-nitrophenyl)serine
glycine + 3-nitrobenzaldehyde
143% of the activity with L-threonine
-
-
?
DL-threo-phenylserine
glycine + benzaldehyde
glycine + 3,4-dihydroxybenzaldehyde
L-threo-3,4-dihydroxyphenylserine
glycine + 3,4-dihydroxybenzaldehyde
L-threo-3,4-dihydroxyphenylserine + L-erythro-3,4-dihydroxyphenylserine
glycine + acetaldehyde
L-threonine
-
-
-
-
r
glycine + glycolaldehyde
L-4-hydroxythreonine
-
low-specificity L-threonine aldolase is involved in a serendipitous pathway that converts 3-phosphohydroxypyruvate, an intermediate in the serine biosynthesis pathway, to L-4-phosphohydroxythreonine, an intermediate in the pyridoxal-5'-phosphate synthesis pathway in a strain of Escherichia coli that lacks 4-phosphoerythronate dehydrogenase
-
-
r
L-4-hydroxythreonine
glycine + glycolaldehyde
-
cleavage of L-4-hydroxythreonine is as efficient as cleavage of L-allo-threonine
-
-
r
L-allo-threonine
glycine + acetaldehyde
L-erythro-phenylserine
glycine + benzaldehyde
L-serine
glycine + formaldehyde
-
-
-
-
?
L-Thr
glycine + acetaldehyde
L-threo-3,4-dihydroxyphenylserine
glycine + 3,4-dihydroxybenzaldehyde
L-threo-beta-3,4-dihydroxyphenylserine
glycine + 3,4-dihydroxybenzaldehyde
L-threo-beta-3,4-methylenedioxyphenylserine
?
L-threo-phenylserine
glycine + benzaldehyde
-
-
-
?
L-threonine
glycine + acetaldehyde
N-(S)-benzyloxycarbonyl-alaninal + glycine
(2S,3R,4S)-2-amino-4-(benzyloxycarbonylamino)-3-hydroxypentanoic acid
N-(S)-benzyloxycarbonyl-alaninal + glycine
(2S,3S,4S)-2-amino-4-(benzyloxycarbonylamino)-3-hydroxypentanoic acid
-
conversion: 54%, glycine concentration: 140 mM, reaction temperature: 25°C, yield: 27%, L-erythro/L-threo: 18:82
-
-
?
N-benzyloxycarbonyl-3-aminopropanal + glycine
(2S,3R)-2-amino-5-(benzyloxycarbonylamino)-3-hydroxypentanoic acid
N-benzyloxycarbonyl-3-aminopropanal + glycine
(2S,3S)-2-amino-5-(benzyloxycarbonylamino)-3-hydroxypentanoic acid
N-benzyloxycarbonyl-glycinal + glycine
(2S,3R)-2-amino-4-(benzyloxycarbonylamino)-3-hydroxybutanoic acid
N-benzyloxycarbonyl-glycinal + glycine
(2S,3S)-2-amino-4-(benzyloxycarbonylamino)-3-hydroxybutanoic acid
additional information
?
-
(R)-N-Cbz-alaninal + glycine
(2S,3R,4R)-2-amino-4-(benzyloxycarbonylamino)-3-hydroxypentanoic acid
-
conversion: 40%, glycine concentration: 70 mM, reaction temperature: 4°C, yield: 30%, L-erythro/L-threo: 16:84
-
-
?
(R)-N-Cbz-alaninal + glycine
(2S,3R,4R)-2-amino-4-(benzyloxycarbonylamino)-3-hydroxypentanoic acid
-
conversion: 60%, glycine concentration: 70 mM, reaction temperature: 4°C, yield: 30%, L-erythro/L-threo: 100:0
-
-
?
benzyloxyacetaldehyde + glycine
(2S,3R)-2-amino-4-(benzyloxy)-3-hydroxybutanoic acid
-
conversion: 45%, glycine concentration: 140 mM, reaction temperature: 25°C, yield: 30%, L-erythro/L-threo: 40:60
-
-
?
benzyloxyacetaldehyde + glycine
(2S,3R)-2-amino-4-(benzyloxy)-3-hydroxybutanoic acid
-
conversion: 68%, glycine concentration: 70 mM, reaction temperature: 4°C, yield: 40%, L-erythro/L-threo: 97:3
-
-
?
DL-threo-phenylserine
glycine + benzaldehyde
-
-
-
?
DL-threo-phenylserine
glycine + benzaldehyde
180% of the activity with L-threonine
-
-
?
glycine + 3,4-dihydroxybenzaldehyde
L-threo-3,4-dihydroxyphenylserine
-
-
-
-
r
glycine + 3,4-dihydroxybenzaldehyde
L-threo-3,4-dihydroxyphenylserine
-
L-threo-3,4-dihydroxyphenylserine synthesis activity is dramatically decreased when the condensation reaction is repeated
-
-
?
glycine + 3,4-dihydroxybenzaldehyde
L-threo-3,4-dihydroxyphenylserine
-
L-threo-3,4-dihydroxyphenylserine synthesis activity is dramatically decreased when the condensation reaction is repeated
-
-
?
glycine + 3,4-dihydroxybenzaldehyde
L-threo-3,4-dihydroxyphenylserine + L-erythro-3,4-dihydroxyphenylserine
-
-
-
-
r
glycine + 3,4-dihydroxybenzaldehyde
L-threo-3,4-dihydroxyphenylserine + L-erythro-3,4-dihydroxyphenylserine
-
-
-
-
r
L-allo-threonine
glycine + acetaldehyde
-
-
-
?
L-allo-threonine
glycine + acetaldehyde
-
-
-
?
L-allo-threonine
glycine + acetaldehyde
-
-
-
-
?
L-allo-threonine
glycine + acetaldehyde
-
-
-
-
r
L-allo-threonine
glycine + acetaldehyde
-
-
-
?
L-allo-threonine
glycine + acetaldehyde
-
-
-
r
L-allo-threonine
glycine + acetaldehyde
291% of the activity with L-threonine
-
-
?
L-allo-threonine
glycine + acetaldehyde
-
-
-
-
?
L-allo-threonine
glycine + acetaldehyde
-
-
-
r
L-allo-threonine
glycine + acetaldehyde
-
-
-
r
L-allo-threonine
glycine + acetaldehyde
-
-
-
?
L-allo-threonine
glycine + acetaldehyde
-
-
-
-
r
L-erythro-phenylserine
glycine + benzaldehyde
-
-
-
?
L-erythro-phenylserine
glycine + benzaldehyde
-
-
-
?
L-phenylserine
?
-
-
-
-
?
L-phenylserine
?
-
-
-
-
?
L-Thr
glycine + acetaldehyde
-
-
-
-
?
L-Thr
glycine + acetaldehyde
-
-
-
-
?
L-threo-3,4-dihydroxyphenylserine
glycine + 3,4-dihydroxybenzaldehyde
-
-
-
-
?
L-threo-3,4-dihydroxyphenylserine
glycine + 3,4-dihydroxybenzaldehyde
-
-
-
-
?
L-threo-beta-3,4-dihydroxyphenylserine
glycine + 3,4-dihydroxybenzaldehyde
-
-
-
?
L-threo-beta-3,4-dihydroxyphenylserine
glycine + 3,4-dihydroxybenzaldehyde
-
-
-
?
L-threo-beta-3,4-methylenedioxyphenylserine
?
-
-
-
?
L-threo-beta-3,4-methylenedioxyphenylserine
?
-
-
-
?
L-threonine
glycine + acetaldehyde
-
-
r
L-threonine
glycine + acetaldehyde
-
-
r
L-threonine
glycine + acetaldehyde
-
-
-
?
L-threonine
glycine + acetaldehyde
-
-
-
?
L-threonine
glycine + acetaldehyde
-
-
-
-
?
L-threonine
glycine + acetaldehyde
-
-
-
-
r
L-threonine
glycine + acetaldehyde
-
-
-
?
L-threonine
glycine + acetaldehyde
-
-
-
r
L-threonine
glycine + acetaldehyde
-
-
-
?
L-threonine
glycine + acetaldehyde
-
-
-
-
?
L-threonine
glycine + acetaldehyde
-
-
-
r
L-threonine
glycine + acetaldehyde
-
-
-
r
L-threonine
glycine + acetaldehyde
-
-
-
r
L-threonine
glycine + acetaldehyde
-
-
-
-
r
N-(S)-benzyloxycarbonyl-alaninal + glycine
(2S,3R,4S)-2-amino-4-(benzyloxycarbonylamino)-3-hydroxypentanoic acid
-
conversion: 54%, glycine concentration: 140 mM, reaction temperature: 25°C, yield: 27%, L-erythro/L-threo: 18:82
-
-
?
N-(S)-benzyloxycarbonyl-alaninal + glycine
(2S,3R,4S)-2-amino-4-(benzyloxycarbonylamino)-3-hydroxypentanoic acid
-
conversion: 48%, glycine concentration: 280 mM, reaction temperature: 4°C, yield: 30%, L-erythro/L-threo: 100:0
-
-
?
N-benzyloxycarbonyl-3-aminopropanal + glycine
(2S,3R)-2-amino-5-(benzyloxycarbonylamino)-3-hydroxypentanoic acid
-
conversion: 49%, glycine concentration: 70 mM, reaction temperature: 25°C, yield: 11%, L-erythro/L-threo: 50:50
-
-
?
N-benzyloxycarbonyl-3-aminopropanal + glycine
(2S,3R)-2-amino-5-(benzyloxycarbonylamino)-3-hydroxypentanoic acid
-
conversion: 34%, glycine concentration: 70 mM, reaction temperature: 25°C, yield: 10%, L-erythro/L-threo: 50:50
-
-
?
N-benzyloxycarbonyl-3-aminopropanal + glycine
(2S,3S)-2-amino-5-(benzyloxycarbonylamino)-3-hydroxypentanoic acid
-
conversion: 49%, glycine concentration: 70 mM, reaction temperature: 25°C, yield: 11%, L-erythro/L-threo: 50:50
-
-
?
N-benzyloxycarbonyl-3-aminopropanal + glycine
(2S,3S)-2-amino-5-(benzyloxycarbonylamino)-3-hydroxypentanoic acid
-
conversion: 20%, glycine concentration: 70 mM, reaction temperature: 4°C, yield: 3%, L-erythro/L-threo: 100:0
-
-
?
N-benzyloxycarbonyl-glycinal + glycine
(2S,3R)-2-amino-4-(benzyloxycarbonylamino)-3-hydroxybutanoic acid
-
conversion: 60%, glycine concentration: 140 mM, reaction temperature: 25°C, yield: 18%, L-erythro/L-threo: 30:70
-
-
?
N-benzyloxycarbonyl-glycinal + glycine
(2S,3R)-2-amino-4-(benzyloxycarbonylamino)-3-hydroxybutanoic acid
-
conversion: 35%, glycine concentration: 70 mM, reaction temperature: 4°C, yield: 13%, L-erythro/L-threo: 86:14
-
-
?
N-benzyloxycarbonyl-glycinal + glycine
(2S,3S)-2-amino-4-(benzyloxycarbonylamino)-3-hydroxybutanoic acid
-
conversion: 60%, glycine concentration: 140 mM, reaction temperature: 25°C, yield: 18%, L-erythro/L-threo: 30:70
-
-
?
N-benzyloxycarbonyl-glycinal + glycine
(2S,3S)-2-amino-4-(benzyloxycarbonylamino)-3-hydroxybutanoic acid
-
conversion: 35%, glycine concentration: 70 mM, reaction temperature: 4°C, yield: 13%, L-erythro/L-threo: 86:14
-
-
?
additional information
?
-
glycine metabolism
-
?
additional information
?
-
-
glycine metabolism
-
?
additional information
?
-
glycine metabolism
-
?
additional information
?
-
-
by manipulating reaction parameters, SHMT yields exclusively L-erythro diastereomers in 34-60% conversion. SHMT is among the most stereoselective L-threonine aldolases described. This is due to its activity-temperature dependence: at 4°C SHMT has high synthetic activity but negligible retro-aldol activity on l-threonine. Thus, the kinetic l-erythro isomer is largely favored and the reactions are virtually irreversible, highly stereoselective, and in turn, give excellent conversion
-
-
?
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0.24
DL-erythro-phenylserine
pH 8.0, 30°C
23.6
DL-threo-(3-methylsulfonylphenyl)serine
pH 7.0, 37°C
21.5
DL-threo-(3-nitrophenyl)serine
pH 7.0, 37°C
0.12 - 19.2
DL-threo-phenylserine
0.027
L-4-hydroxythreonine
-
pH 8.0, 25°C
0.052 - 31
L-allo-threonine
10.2
L-erythro-phenylserine
pH 8.0, 30°C
0.000002 - 0.0000026
L-phenylserine
0.0002 - 0.00023
L-threo-3,4-dihydroxyphenylserine
8.3
L-threo-beta-3,4-dihydroxyphenylserine
pH 8.0, 30°C
7.4
L-threo-beta-3,4-methylenedioxyphenylserine
pH 8.0, 30°C
7.3
L-threo-phenylserine
pH 8.0, 30°C
0.12
DL-threo-phenylserine
pH 8.0, 30°C
19.2
DL-threo-phenylserine
pH 7.0, 37°C
0.052
L-allo-threonine
-
pH 8.0, 25°C
0.2
L-allo-threonine
-
mutant H126NF, pH 7.0, 30°C
0.22
L-allo-threonine
pH 8.0, 30°C
0.24
L-allo-threonine
pH 7.0, 30°C, wild-type enzyme
0.24
L-allo-threonine
-
wild-type, pH 7.0, 30°C
0.31
L-allo-threonine
pH 7.0, 30°C, mutant enzyme F87A
0.41
L-allo-threonine
pH 7.0, 30°C, mutant enzyme F87D
0.69
L-allo-threonine
wild-type, pH 8.0, 30°C
0.96
L-allo-threonine
-
mutant H126N, pH 7.0, 30°C
1 - 2
L-allo-threonine
mutant D95L, pH 8.0, 30°C
1.2
L-allo-threonine
pH 7.0, 30°C, mutant enzyme K222A
1.3
L-allo-threonine
-
mutant F87A, pH 7.0, 30°C
1.5
L-allo-threonine
pH 7.0, 37°C
1.7
L-allo-threonine
-
mutant F87D, pH 7.0, 30°C
1.7
L-allo-threonine
-
mutant H83N, pH 7.0, 30°C
2.5
L-allo-threonine
mutant D95W, pH 8.0, 30°C
2.7
L-allo-threonine
mutant D95Y, pH 8.0, 30°C
2.9
L-allo-threonine
mutant D95G/E96G, pH 8.0, 30°C
4.4
L-allo-threonine
mutant D95Y/E96T, pH 8.0, 30°C
5
L-allo-threonine
-
mutant K222A, pH 7.0, 30°C
7
L-allo-threonine
-
mutant H83F, pH 7.0, 30°C
7.1
L-allo-threonine
mutant D95N/E96S, pH 8.0, 30°C
7.4
L-allo-threonine
pH 7.0, 30°C, mutant enzyme H83F/H126F
10
L-allo-threonine
pH 8.0, 30°C
11
L-allo-threonine
mutant D95C, pH 8.0, 30°C
14.6
L-allo-threonine
pH 8.0, 30°C
31
L-allo-threonine
-
mutant H83F/H126F, pH 7.0, 30°C
0.000002
L-phenylserine
-
recombinant wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0)
0.0000026
L-phenylserine
-
mutant enzyme H177Y, in 50 mM Tris-HCl buffer (pH 8.0)
0.00016
L-Thr
-
mutant enzyme H177Y, in 50 mM Tris-HCl buffer (pH 8.0)
0.00018
L-Thr
-
recombinant wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0)
0.0002
L-threo-3,4-dihydroxyphenylserine
-
recombinant wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0)
0.00023
L-threo-3,4-dihydroxyphenylserine
-
mutant enzyme H177Y, in 50 mM Tris-HCl buffer (pH 8.0)
0.4
L-threonine
-
mutant F87A, pH 7.0, 30°C
1 - 3
L-threonine
mutant D95G/E96G, pH 8.0, 30°C
1.1
L-threonine
-
mutant H83F/H126F, pH 7.0, 30°C
1.3
L-threonine
-
mutant F87D, pH 7.0, 30°C
1.7
L-threonine
-
mutant H126F, pH 7.0, 30°C
2.85
L-threonine
pH 8.0, 30°C
3.7
L-threonine
-
mutant K222A, pH 7.0, 30°C
4
L-threonine
-
pH 8.0, 25°C
7
L-threonine
-
mutant H83F, pH 7.0, 30°C
8.7
L-threonine
pH 7.0, 30°C, mutant enzyme F87A
13.6
L-threonine
wild-type, pH 8.0, 30°C
14.7
L-threonine
pH 8.0, 30°C
19.4
L-threonine
pH 7.0, 30°C, wild-type enzyme
19.4
L-threonine
-
wild-type, pH 7.0, 30°C
21
L-threonine
pH 7.0, 30°C, mutant enzyme H83F/H126F
24.9
L-threonine
pH 7.0, 30°C, mutant enzyme F87D
32
L-threonine
mutant D95N/E96S, pH 8.0, 30°C
38
L-threonine
-
mutant H83N, pH 7.0, 30°C
43.1
L-threonine
pH 7.0, 37°C
44
L-threonine
mutant D95C, pH 8.0, 30°C
44
L-threonine
mutant D95W, pH 8.0, 30°C
50
L-threonine
mutant D95M, pH 8.0, 30°C
53
L-threonine
mutant D95L, pH 8.0, 30°C
55
L-threonine
pH 8.0, 30°C
61
L-threonine
-
mutant H126N, pH 7.0, 30°C
63
L-threonine
mutant D95Y, pH 8.0, 30°C
72
L-threonine
pH 7.0, 30°C, mutant enzyme K222A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.44
L-4-hydroxythreonine
-
pH 8.0, 25°C
0.028 - 41
L-allo-threonine
0.000107 - 0.000113
L-phenylserine
0.00022 - 0.00023
L-threo-3,4-dihydroxyphenylserine
0.028
L-allo-threonine
pH 7.0, 30°C, mutant enzyme H83F/H126F
0.06
L-allo-threonine
-
mutant H83F, pH 7.0, 30°C
0.2
L-allo-threonine
mutant D95N/E96S, pH 8.0, 30°C
1.28
L-allo-threonine
-
mutant H83N, pH 7.0, 30°C
1.33
L-allo-threonine
pH 7.0, 30°C, mutant enzyme K222A
1.95
L-allo-threonine
pH 7.0, 30°C, mutant enzyme F87D
2.7
L-allo-threonine
pH 7.0, 30°C, mutant enzyme F87A
3
L-allo-threonine
mutant D95Y/E96T, pH 8.0, 30°C
3.2
L-allo-threonine
-
pH 8.0, 25°C
3.55
L-allo-threonine
pH 7.0, 30°C, wild-type enzyme
3.55
L-allo-threonine
-
wild-type, pH 7.0, 30°C
7.82
L-allo-threonine
-
mutant H126N, pH 7.0, 30°C
8.6
L-allo-threonine
mutant D95G/E96G, pH 8.0, 30°C
9.02
L-allo-threonine
-
mutant H126NF, pH 7.0, 30°C
19
L-allo-threonine
mutant D95C, pH 8.0, 30°C
19
L-allo-threonine
mutant D95W, pH 8.0, 30°C
20
L-allo-threonine
wild-type, pH 8.0, 30°C
20
L-allo-threonine
mutant D95Y, pH 8.0, 30°C
22
L-allo-threonine
mutant D95L, pH 8.0, 30°C
41
L-allo-threonine
pH 8.0, 30°C
0.000107
L-phenylserine
-
recombinant wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0)
0.000113
L-phenylserine
-
mutant enzyme H177Y, in 50 mM Tris-HCl buffer (pH 8.0)
0.0178
L-Thr
-
mutant enzyme H177Y, in 50 mM Tris-HCl buffer (pH 8.0)
0.0195
L-Thr
-
recombinant wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0)
0.00022
L-threo-3,4-dihydroxyphenylserine
-
recombinant wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0)
0.00023
L-threo-3,4-dihydroxyphenylserine
-
mutant enzyme H177Y, in 50 mM Tris-HCl buffer (pH 8.0)
0.0073
L-threonine
pH 7.0, 30°C, mutant enzyme H83F/H126F
0.02
L-threonine
-
mutant H83F, pH 7.0, 30°C
0.2
L-threonine
mutant D95N/E96S, pH 8.0, 30°C
0.28
L-threonine
-
mutant H83N, pH 7.0, 30°C
0.33
L-threonine
pH 7.0, 30°C, mutant enzyme F87D
0.6
L-threonine
mutant D95G/E96G, pH 8.0, 30°C
0.72
L-threonine
pH 7.0, 30°C, mutant enzyme F87A
0.72
L-threonine
pH 7.0, 30°C, mutant enzyme K222A
1.1
L-threonine
-
pH 8.0, 25°C
1.87
L-threonine
pH 7.0, 30°C, wild-type enzyme
1.87
L-threonine
-
wild-type, pH 7.0, 30°C
3
L-threonine
mutant D95C, pH 8.0, 30°C
3.3
L-threonine
wild-type, pH 8.0, 30°C
3.5
L-threonine
mutant D95Y, pH 8.0, 30°C
3.6
L-threonine
mutant D95M, pH 8.0, 30°C
3.8
L-threonine
mutant D95L, pH 8.0, 30°C
4.37
L-threonine
-
mutant H126N, pH 7.0, 30°C
6
L-threonine
-
mutant H126F, pH 7.0, 30°C
9.6
L-threonine
mutant D95W, pH 8.0, 30°C
43
L-threonine
pH 8.0, 30°C
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5.3
L-4-hydroxythreonine
-
pH 8.0, 25°C
0.00033 - 45.08
L-allo-threonine
0.0016 - 14.78
L-threonine
0.00033
L-allo-threonine
pH 7.0, 30°C, mutant enzyme H83F/H126F
0.01
L-allo-threonine
-
mutant H83F, pH 7.0, 30°C
0.01
L-allo-threonine
pH 7.0, 30°C, mutant enzyme K222A
0.013
L-allo-threonine
pH 7.0, 30°C, mutant enzyme F87D
0.028
L-allo-threonine
mutant D95N/E96S, pH 8.0, 30°C
0.082
L-allo-threonine
pH 7.0, 30°C, mutant enzyme F87A
0.097
L-allo-threonine
pH 7.0, 30°C, wild-type enzyme
0.68
L-allo-threonine
mutant D95Y/E96T, pH 8.0, 30°C
0.75
L-allo-threonine
-
mutant H83N, pH 7.0, 30°C
1.7
L-allo-threonine
mutant D95C, pH 8.0, 30°C
1.8
L-allo-threonine
mutant D95L, pH 8.0, 30°C
3
L-allo-threonine
mutant D95G/E96G, pH 8.0, 30°C
4.1
L-allo-threonine
pH 8.0, 30°C
6.2
L-allo-threonine
-
pH 8.0, 25°C
7.4
L-allo-threonine
mutant D95Y, pH 8.0, 30°C
7.6
L-allo-threonine
mutant D95W, pH 8.0, 30°C
8.13
L-allo-threonine
-
mutant H126N, pH 7.0, 30°C
14.78
L-allo-threonine
-
wild-type, pH 7.0, 30°C
29
L-allo-threonine
wild-type, pH 8.0, 30°C
45.08
L-allo-threonine
-
mutant H126NF, pH 7.0, 30°C
0.0016
L-threonine
mutant D95Y/E96T, pH 8.0, 30°C
0.0038
L-threonine
pH 7.0, 30°C, mutant enzyme H83F/H126F
0.0063
L-threonine
mutant D95N/E96S, pH 8.0, 30°C
0.01
L-threonine
-
mutant H83N, pH 7.0, 30°C
0.046
L-threonine
mutant D95G/E96G, pH 8.0, 30°C
0.056
L-threonine
mutant D95Y, pH 8.0, 30°C
0.068
L-threonine
mutant D95C, pH 8.0, 30°C
0.07
L-threonine
-
mutant H126N, pH 7.0, 30°C
0.072
L-threonine
mutant D95L, pH 8.0, 30°C
0.072
L-threonine
mutant D95M, pH 8.0, 30°C
0.1
L-threonine
-
wild-type, pH 7.0, 30°C
0.218
L-threonine
mutant D95W, pH 8.0, 30°C
0.24
L-threonine
wild-type, pH 8.0, 30°C
0.78
L-threonine
pH 8.0, 30°C
1.1
L-threonine
pH 7.0, 30°C, mutant enzyme K222A
2.8
L-threonine
-
pH 8.0, 25°C
3.53
L-threonine
-
mutant H126F, pH 7.0, 30°C
4.75
L-threonine
pH 7.0, 30°C, mutant enzyme F87D
8.6
L-threonine
pH 7.0, 30°C, mutant enzyme F87A
14.78
L-threonine
pH 7.0, 30°C, wild-type enzyme
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D176E
500fold decrease in catalytic efficiency
D95C
less than 10% of catalytic efficiency of wild-type
D95H/E96G
less than 10% of catalytic efficiency of wild-type
D95L
less than 10% of catalytic efficiency of wild-type
D95M
less than 5% of catalytic efficiency of wild-type
D95N/E96S
less than 5% of catalytic efficiency of wild-type
D95W
less than 2% of catalytic efficiency of wild-type
D95Y
less than 5% of catalytic efficiency of wild-type
D95Y/E96T
less than 10% of catalytic efficiency of wild-type
D176E
-
500fold decrease in catalytic efficiency
-
D95C
-
less than 10% of catalytic efficiency of wild-type
-
D95L
-
less than 10% of catalytic efficiency of wild-type
-
D95M
-
less than 5% of catalytic efficiency of wild-type
-
D95Y
-
less than 5% of catalytic efficiency of wild-type
-
H126F
-
300% of wild-type activity,reduced preference for the erythro-substrate
H126N
-
60% of wild-type activity
H83F
-
less than 1% of wild-type activity, reduced preference for the erythro-substrate
H83N
-
less than 10% of wild-type activity
industry
biocatalysis using threonine aldolases opens up a way to synthesise beta-hydroxy-alpha-amino acids in one step. Dichiral beta-hydroxy-alpha-amino acids are a highly valuable class of compounds from which pharmaceutically active intermediates for the synthesis of e.g. beta-sympathomimetic drugs. Methods to immobilise the L-low specificity threonine aldolase of Escherichia coli are studied. The entrapment of the enzyme into a porous network of orthosilicate appears to be the most promising method
synthesis
biocatalysis using threonine aldolases opens up a way to synthesise beta-hydroxy-alpha-amino acids in one step. Dichiral beta-hydroxy-alpha-amino acids are a highly valuable class of compounds from which pharmaceutically active intermediates for the synthesis of e.g. beta-sympathomimetic drugs. Methods to immobilise the L-low specificity threonine aldolase of Escherichia coli are studied. The entrapment of the enzyme into a porous network of orthosilicate appears to be the most promising method
F87A
-
no change in the ration of cleavage of L-threonine to L-allo-threonine
-
F87D
-
mutation doubles the preference of the enzyme for L-allo-threonine
-
H126F
-
300% of wild-type activity,reduced preference for the erythro-substrate
-
H126N
-
60% of wild-type activity
-
K222A
-
slight decrease in kcat and slight increase in Km values for both L-threonine and L-allo-threonine
-
K207A
the mutant enzyme shows no detectable enzyme activity. The mutant enzyme show the disappearance of the absorption maximum at 420 nm, indicating that the Schiff base linkage between the epsilon-amino group of the active-site lysine residue and the pyridoxal 5'-phosphate cofactor aldehyde group of the wild type is not present in the mutant enzyme
K207R
the mutant enzyme shows a specific activity of about 1000 times lower than that of the wild-type enzyme. The mutant enzyme show the disappearance of the absorption maximum at 420 nm, indicating that the Schiff base linkage between the epsilon-amino group of the active-site lysine residue and the pyridoxal 5'-phosphate cofactor aldehyde group of the wild type is not present in the mutant enzyme
K207A
-
the mutant enzyme shows no detectable enzyme activity. The mutant enzyme show the disappearance of the absorption maximum at 420 nm, indicating that the Schiff base linkage between the epsilon-amino group of the active-site lysine residue and the pyridoxal 5'-phosphate cofactor aldehyde group of the wild type is not present in the mutant enzyme
-
K207R
-
the mutant enzyme shows a specific activity of about 1000 times lower than that of the wild-type enzyme. The mutant enzyme show the disappearance of the absorption maximum at 420 nm, indicating that the Schiff base linkage between the epsilon-amino group of the active-site lysine residue and the pyridoxal 5'-phosphate cofactor aldehyde group of the wild type is not present in the mutant enzyme
-
A169T
-
stability-enhanced mutant, half life at 63°C is 3.7 min
D104N
-
stability-enhanced mutant, half life at 63°C is 5.8 min
F18I
-
stability-enhanced mutant, half life at 63°C is 5.0 min, the specific activity is decreased by 45% compared to the wild type enzyme
H177Y
-
stability-enhanced mutant, half life at 63°C is 14.6 min
R241C/A287V
-
the mutations dramatically increase the diastereoselectivity of the reverse aldol condensation activity for L-threo-3,4-dihydroxyphenylserine
V86I/R241C/Y306C
-
the mutations dramatically increase the diastereoselectivity of the reverse aldol condensation activity for L-threo-3,4-dihydroxyphenylserine
Y34C
-
the mutation dramatically increases the diastereoselectivity of the reverse aldol condensation activity for L-threo-3,4-dihydroxyphenylserine
Y39C/Y306C
-
the mutations dramatically increase the diastereoselectivity of the reverse aldol condensation activity for L-threo-3,4-dihydroxyphenylserine
Y39C/Y306C/A48T
-
the mutations dramatically increase the diastereoselectivity of the reverse aldol condensation activity for L-threo-3,4-dihydroxyphenylserine
Y39C/Y306C/R316C
-
the mutations dramatically increase the diastereoselectivity of the reverse aldol condensation activity for L-threo-3,4-dihydroxyphenylserine
A169T
-
stability-enhanced mutant, half life at 63°C is 3.7 min
-
D104N
-
stability-enhanced mutant, half life at 63°C is 5.8 min
-
F18I
-
stability-enhanced mutant, half life at 63°C is 5.0 min, the specific activity is decreased by 45% compared to the wild type enzyme
-
H177Y
-
stability-enhanced mutant, half life at 63°C is 14.6 min
-
R241C/A287V
-
the mutations dramatically increase the diastereoselectivity of the reverse aldol condensation activity for L-threo-3,4-dihydroxyphenylserine
-
V86I/R241C/Y306C
-
the mutations dramatically increase the diastereoselectivity of the reverse aldol condensation activity for L-threo-3,4-dihydroxyphenylserine
-
Y34C
-
the mutation dramatically increases the diastereoselectivity of the reverse aldol condensation activity for L-threo-3,4-dihydroxyphenylserine
-
Y39C/Y306C
-
the mutations dramatically increase the diastereoselectivity of the reverse aldol condensation activity for L-threo-3,4-dihydroxyphenylserine
-
Y39C/Y306C/A48T
-
the mutations dramatically increase the diastereoselectivity of the reverse aldol condensation activity for L-threo-3,4-dihydroxyphenylserine
-
F87A
-
no change in the ration of cleavage of L-threonine to L-allo-threonine
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
F87D
-
mutation doubles the preference of the enzyme for L-allo-threonine
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
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
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
K222A
-
slight decrease in kcat and slight increase in Km values for both L-threonine and L-allo-threonine
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
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Threonine aldolase from Candida humicola. II. Purification, crystallization and properties
Biochim. Biophys. Acta
258
779-790
1972
Vanrija humicola
brenda
Yamada, H.; Kumagai, H.; Nagate, T.; Yoshida, H.
Crystalline threonine aldolase from Candida humicola
Biochem. Biophys. Res. Commun.
39
53-58
1970
Vanrija humicola
brenda
Liu, J.Q.; Nagata, S.; Dairi, T.; Misono, H.; Shimizu, S.; Yamada, H.
The GLY1 gene of Saccharomyces cerevisiae encodes a low-specific L-threonine aldolase that catalyzes cleavage of L-allo-threonine and L-threonine to glycine
Eur. J. Biochem.
245
289-293
1997
Saccharomyces cerevisiae (P37303)
brenda
Liu, J.Q.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.; Yamada, H.
Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli
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255
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1998
Escherichia coli (P75823), Escherichia coli
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Gene cloning, nucleotide sequencing, and purification and characterization of the low-specificity L-threonine aldolase from Pseudomonas sp. strain NCIMB 10558
Appl. Environ. Microbiol.
64
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1998
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brenda
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Glycine metabolism in Candida albicans: characterization of the serine hydroxymethyltransferase (SHM1, SHM2) and threonine aldolase (GLY1) genes
Yeast
16
167-175
2000
Candida albicans (O13427), Candida albicans, Candida albicans SGY269 (O13427)
brenda
Balk, S.H.; Yoshioka, H.; Yukawa, H.; Harayama, S.
Synthesis of L-threo-3,4-dihydroxyphenylserine (L-threo-DOPS) with thermostabilized low-specific L-threonine aldolase from Streptomyces coelicolor A3(2)
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17
721-727
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Streptomyces coelicolor, Streptomyces coelicolor A3(2)
brenda
Baik, S.H.; Yoshioka, H.
Enhanced synthesis of L-threo-3,4-dihydroxyphenylserine by high-density whole-cell biocatalyst of recombinant L-threonine aldolase from Streptomyces avelmitilis
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31
443-448
2009
Streptomyces avermitilis
brenda
Gutierrez, M.L.; Garrabou, X.; Agosta, E.; Servi, S.; Parella, T.; Joglar, J.; Clapes, P.
Serine hydroxymethyl transferase from Streptococcus thermophilus and L-threonine aldolase from Escherichia coli as stereocomplementary biocatalysts for the synthesis of beta-hydroxy-alpha,omega-diamino acid derivatives
Chemistry
14
4647-4656
2008
Escherichia coli, Streptococcus thermophilus
brenda
Gwon, H.J.; Baik, S.H.
Diastereoselective synthesis of L-threo-3,4-dihydroxyphenylserine by low-specific L-threonine aldolase mutants
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32
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2010
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
brenda
Kim, J.; Kershner, J.P.; Novikov, Y.; Shoemaker, R.K.; Copley, S.D.
Three serendipitous pathways in E. coli can bypass a block in pyridoxal-5'-phosphate synthesis
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6
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2010
Escherichia coli
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Zhao, G.H.; Li, H.; Liu, W.; Zhang, W.G.; Zhang, F.; Liu, Q.; Jiao, Q.C.
Preparation of optically active beta-hydroxy-alpha-amino acid by immobilized Escherichia coli cells with serine hydroxymethyl transferase activity
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40
215-220
2011
Escherichia coli (P0A825), Escherichia coli
brenda
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
FEBS J.
281
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2014
Escherichia coli, Escherichia coli WV_060327
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Optimal production of L-threo-2,3-dihydroxyphenylserine (L-threo-DOPS) on a large scale by diastereoselectivity-enhanced variant of L-threonine aldolase expressed in Escherichia coli
Prep. Biochem. Biotechnol.
42
143-154
2012
Sinorhizobium arboris (A0T1V9)
brenda
Giger, L.; Toscano, M.; Bouzon, M.; Marlière, P.; Hilvert, D.
A novel genetic selection system for PLP-dependent threonine aldolases
Tetrahedron
68
7549-7557
2012
Caulobacter vibrioides (Q9A3V8), Caulobacter vibrioides CB15 (Q9A3V8)
-
brenda
Remesh, S.G.; Ghatge, M.S.; Ahmed, M.H.; Musayev, F.N.; Gandhi, A.; Chowdhury, N.; di Salvo, M.L.; Kellogg, G.E.; Contestabile, R.; Schirch, V.; Safo, M.K.
Molecular basis of E. coli L-threonine aldolase catalytic inactivation at low pH
Biochim. Biophys. Acta
1854
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2015
Escherichia coli
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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
FEBS J.
281
129-145
2014
Escherichia coli (P75823)
brenda
Kurjatschij, S.; Katzberg, M.; Bertau, M.
Production and properties of threonine aldolase immobilisates
J. Mol. Catal. B
103
3-9
2014
Escherichia coli (P75823)
-
brenda