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2 pyruvate
erythrulose
-
-
-
?
3-formylbenzoic acid + pyruvate
3-(2-oxopropanoyl)benzoate + CO2
-
-
-
?
3-formylbenzoic acid + pyruvate
3-(2-oxopropanoyl)benzoic acid + CO2
-
-
-
ir
3-hydroxypyruvate + n-pentanal
1,3-dihydroxy-2-heptanone + CO2
3% yield after 1 h (92% (S)), 12% yield after 3 h (87% (S))
-
-
ir
3-hydroxypyruvate + propanal
1,3-dihydroxy-2-pentanone + CO2
12% yield after 1 h (57% (S)), 32% yield after 3 h (53% (S))
-
-
ir
beta-hydroxypyruvate + glycolaldehyde
L-erythrulose + CO2
-
-
-
?
D-erythrose 4-phosphate + D-xylulose 5-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 6-phosphate + D-ribose 5-phosphate
D-erythrose 4-phosphate + sedoheptulose 7-phosphate
-
-
-
?
D-glyceraldehyde 3-phosphate + D-fructose 6-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
?
D-ribose-5-phosphate + L-erythrulose
D-sedoheptulose 7-phosphate + glycolaldehyde
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
glycolaldehyde + pyruvate
3,4-dihydroxy-2-butanone + CO2
-
-
-
?
hexanal + 2-oxoheptanoic acid
7-hydroxydodecan-6-one + CO2
-
-
-
?
hexanal + pyruvate
2-hydroxyheptanal + CO2
-
-
-
?
hydroxypyruvate + D-ribose-5-phosphate
D-sedoheptulose 7-phosphate
-
-
-
ir
hydroxypyruvate + glycolaldehyde
L-erythrulose + ?
-
-
-
?
L-arabinose + lithium beta-hydroxypyruvate
L-gluco-heptulose + CO2 + Li+
48% conversion after 24 h
-
-
?
pentanal + 2-oxohexanoic acid
6-hydroxydecan-5-one + CO2
-
-
-
?
pentanal + pyruvate
2-hydroxyhexanal + CO2
-
-
-
?
propionaldehyde + 2-oxobutanoic acid
4-hydroxyhexan-3-one + CO2
-
-
-
?
propionaldehyde + pyruvate
2-hydroxybutanal + CO2
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
2 propanal + 2 lithium beta-hydroxypyruvate
(3S)-1,3-dihydroxypentan-2-one + (3R)-1,3-dihydroxypentan-2-one + 2 CO2 + 2 Li+
-
use of lithium beta-hydroxypyruvate as a donor renders the reaction irreversible
wild-type, 58% enantiomeric excess for 3S-product
-
r
3-formylbenzoic acid + hydroxypyruvate
3-(1,3-dihydroxy-2-oxopropyl)benzoic acid + CO2
-
-
-
-
?
3-hydroxybenzaldehyde + hydroxypyruvate
1,3-dihydroxy-1-(3-hydroxyphenyl)propan-2-one + CO2
-
-
-
-
?
4-formylbenzoic acid + hydroxypyruvate
4-(1,3-dihydroxy-2-oxopropyl)benzoic acid + CO2
-
-
-
-
?
beta-hydroxypyruvate + glycolaldehyde
L-erythrulose + CO2
-
-
-
-
?
D-erythrose + ?
?
-
-
-
-
?
D-erythrose 4-phosphate + ?
?
-
-
-
-
?
D-glyceraldehyde 3-phosphate + D-fructose 6-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
DL-glyceraldehyde + ?
?
-
-
-
-
?
DL-glyceraldehyde 3-phosphate + ?
?
-
-
-
-
?
formaldehyde + ?
?
-
-
-
-
?
fructose 6-phosphate + ?
?
-
-
-
-
?
glycolaldehyde + ?
?
-
-
-
-
?
hydroxypyruvate + ?
?
-
-
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
-
-
-
?
hydroxypyruvate + glycolaldehyde
L-erythrulose + ?
-
-
-
-
?
hydroxypyruvate + ribose 5-phosphate
sedoheptulose 7-phosphate + ?
-
-
-
-
?
Li-hydroxypyruvate + propionaldehyde
1,3-dihydroxypentan-2-one + ?
-
-
-
-
?
lithium beta-hydroxypyruvate + glycolaldehyde
L-erythrulose + ?
-
-
-
-
?
propanal + glycolaldehyde
(3S)-1,3-dihydroxypentan-2-one
-
-
-
-
?
sedoheptulose 7-phosphate + ?
?
-
-
-
-
?
additional information
?
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ping pong bi bi mechanism
-
-
?
additional information
?
-
the wild type enzyme shows no activity with 3-formylbenzoic acid, 4-formylbenzoic acid and 3-hydroxybenzaldehyde
-
-
-
additional information
?
-
-
the wild type enzyme shows no activity with 3-formylbenzoic acid, 4-formylbenzoic acid and 3-hydroxybenzaldehyde
-
-
-
additional information
?
-
-
low cost, rapid colorimetric transketolase assay, able to detect value above 8% bioconversion using non-alpha-hydroxylated aldehydes as acceptor substrates. The assay is significantly faster and more convenient to use than HPLC and can be used with a range of aliphatic and aromatic aldehydes. In addition, analysis of the alpha,alpha'-dihydroxyketone produced in the bioconversion can be quantified using this assay system with high-throughput. Furthermore, this method has the potential to be used to screen other chemical reactions or bioconversions leading to the formation of products possessing a 2-hydroxyketone motif
-
-
?
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0.0012
-
mutant R520I, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.0014
-
mutant S188T, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.0018
-
mutant S188R, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.002
-
mutant D259Stop, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.007
-
mutant H461Y, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.008
-
mutant H100A and mutant H100V, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.0086
-
mutant R520G, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.009
-
mutant R520P, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.013
-
mutant H461Q, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.02
-
mutant D469S, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.022
-
mutant S188Q, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.025
-
mutant H26V, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.027
-
mutant A29D, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.028
-
mutant H100I and mutant H26V, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.029
-
wild-type, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.036
-
mutant H26K, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.04
-
mutant H461S, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0. Mutant D469Y, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehydee, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.043
-
mutant R358P, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.05
-
mutant D259G, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.055
-
mutant R358I, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.063
-
mutant H26T, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.066
-
mutant D259A and mutant H26A, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.09
-
mutant H100V, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.1
-
mutant A29E, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.11
-
mutant S188R, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.12
-
mutant D259Stop, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.125
-
mutant D469A, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.127
-
mutant D469Y, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.13
-
mutant H100A and mutant S188T, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.16
-
mutant H26T, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.26
-
mutant H26A, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.31
-
mutant H26K, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.37
-
mutant D469T, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.42
-
mutant R520I, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.43
-
mutant D469S, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.48
-
mutant H461Y, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.52
-
mutant H461Q, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.61
-
mutant D469A, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehydee, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.65
-
wild-type, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.88
-
mutant H100I, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1
-
mutant R358P, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.3
-
mutant D259G, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.37
-
mutant R358I, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.4
-
mutant R520G, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.8
-
mutant A29D, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.95
-
mutant A29E, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
3.14
-
mutant H461S, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.14
-
mutant D469T, mutant R520V and mutant R520Stop, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.14
-
mutant R520Stop, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.5
-
mutant D259A, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.5
-
mutant R520P, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.5
-
mutant S188Q, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
2.3
-
mutant R520Stop, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
2.3
-
mutant R520V, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
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D469E
the mutant shows about 4.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
D469T
the mutant shows activities towards the three benzaldehyde analogues, 3-formylbenzoic acid, 4-formylbenzoic acid and 3-hydroxybenzaldehyde compared to the wild type enzyme
D469T/R520Q
the mutant shows improved activities towards the three benzaldehyde analogues, 3-formylbenzoic acid, 4-formylbenzoic acid and 3-hydroxybenzaldehyde compared to mutant enzyme D469T
F434A
the mutation leads to 53% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal)
F434L
the mutation leads to 74% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
H100F
the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H100L
the mutant shows about 2.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H100Y
the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A
the mutant shows about wild type activity with propionaldehyde and pyruvate
H192P/A282P/I365L/G506A/D469E
the mutant shows about 6.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/D469E/H473S
the mutant shows about 2fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H100L
the mutant shows about 2fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H100L/D469E
the mutant shows about 8fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H100L/D469E/R520Q
the mutant shows about 9fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H100L/D469T
the mutant shows about 1.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H100L/H473N
the mutant shows about 4fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H100L/H473S
the mutant shows about 2.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H473N
the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H473S
the mutant shows about 2.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H261A
the mutation leads to 75% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
H261F
the mutation leads to 33% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
H261G
the mutation leads to 59% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
H261L
the mutation leads to 55% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
H261V
the mutation leads to 65% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
H26A
the mutation results in stereoinversion for the formation of 1,3-dihydroxy-2-heptanone, with a lower ee-value of 18% (R) as compared to the wild type enzyme
H26W
the mutant shows an 8fold decreased formation of (R)-1,3-dihydroxy-2-heptanone and an ee-value of 30% (S) after 1 h reaction time
H26Y
the mutant catalyzes the formation of (R)-1,3-dihydroxy-2-heptanone with an ee-value of 98% and a yield of 8% after 1 h
H461Y
the mutant shows about 1.2fold increased activity with L-arabinose compared to the wild type enzyme
H473N
the mutant shows about 2.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H473S
the mutant shows about 1.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
L116I
the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
L382A
the mutation leads to 97% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
L382A/F434A
the mutation leads to 66% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
L382A/F434L
the mutation leads to 10% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
R358I
the mutant shows about 1.2fold increased activity with L-arabinose compared to the wild type enzyme
R358P
the mutant shows about 1.4fold increased activity with L-arabinose compared to the wild type enzyme
R358S
the mutant shows about 1.4fold increased activity with L-arabinose compared to the wild type enzyme
R520P
the mutant shows about 1.5fold increased activity with L-arabinose compared to the wild type enzyme
R520Y
the mutant shows about 2fold increased activity with L-arabinose compared to the wild type enzyme
S385Y/D469T/R520Q
the mutant shows improved activities towards the three benzaldehyde analogues, 3-formylbenzoic acid, 4-formylbenzoic acid and 3-hydroxybenzaldehyde compared to mutant enzyme D469T/R520Q
D259Stop
-
specific activity with propionaldehyde as substrate is lower than for wild-type
D381A
-
56fold less active than the wild-type enzyme. Shows significant destabilization of native and intermediate states of transketolase that can be monitored by changes in the urea denaturation transition mid-points (C1/2) measured by fluorescence
D469A
-
specific activity with propionaldehyde as substrate is 4.3fold greater than for wild-type
D469E
-
formation of (3S)-1,3-dihydroxypentan-2-one in 90% enantiomeric excess in the reaction of propanal + beta-hydroxypyruvate
D469S
-
specific activity with propionaldehyde as substrate is lower than for wild-type
D469T/R520Q
-
the mutant shows 80% activity with 3-formylbenzoic acid, 50% activity with 4-formylbenzoic acid and no activity with 3-hydroxybenzaldehyde compared to mutant enzyme D469T
H100A
-
specific activity with propionaldehyde as substrate is lower than for wild-type
H100I
-
has the same specific activity with propionaldehyde as substrate as the wild-type. Does not improve specific activity towards propionaldehyde
H100V
-
specific activity with propionaldehyde as substrate is lower than for wild-type
H26A
-
specific activity with propionaldehyde as substrate is 2.3fold greater than for wild-type
H26K
-
specific activity with propionaldehyde as substrate is 1.2fold greater than for wild-type
H26T
-
specific activity with propionaldehyde as substrate is 2.2fold greater than for wild-type. 8.5fold improvement in specificity towards propionaldehyde relative to glycolaldehyde
H26V
-
has the same specific activity with propionaldehyde as substrate as the wild-type
H26Y
-
formation of (3R)-1,3-dihydroxypentan-2-one in 88% enantiomeric excess in the reaction of propanal + beta-hydroxypyruvate
H461Q
-
specific activity with propionaldehyde as substrate is lower than for wild-type
H461Y
-
specific activity with propionaldehyde as substrate is lower than for wild-type
R520I
-
specific activity with propionaldehyde as substrate is lower than for wild-type
S188R
-
specific activity with propionaldehyde as substrate is lower than for wild-type
S188T
-
specific activity with propionaldehyde as substrate is lower than for wild-type
S385E
-
the mutation completely removes the substrate inhibition for 3-formylbenzoic acid
S385E/D469T/R520Q
-
the mutant shows 350% activity with 3-formylbenzoic acid, 20% activity with 4-formylbenzoic acid and 600% activity activity with 3-hydroxybenzaldehyde compared to mutant enzyme D469T
S385T/D469T/R520Q
-
the mutant shows 50% activity with 3-formylbenzoic acid, 210% activity with 4-formylbenzoic acid and 1270% activity activity with 3-hydroxybenzaldehyde compared to mutant enzyme D469T
S385Y/D469T/R520Q
-
the mutant shows 50% activity with 3-formylbenzoic acid, 340% activity with 4-formylbenzoic acid and 1240% activity activity with 3-hydroxybenzaldehyde compared to mutant enzyme D469T
Y440A
-
700fold less active than the wild-type enzyme. Shows significant destabilization of native and intermediate states of transketolase that can be monitored by changes in the urea denaturation transition mid-points (C1/2) measured by fluorescence
H26A/H261A
three hydrogen-bonding interactions between the active site and the 3-hydroxyl and 4-hydroxyl groups of the intermediate cannot be formed when compared to the wild-type
H26A/H261A
the mutation leads to 54% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal)
A29D
-
specific activity is 2.7fold greater than for the wild-type
A29D
-
specific activity with propionaldehyde as substrate is lower than for wild-type
A29E
-
specific activity is 3fold greater than for the wild-type
A29E
-
specific activity with propionaldehyde as substrate is 3.4fold greater than for wild-type
D259A
-
specific activity is 2.3fold greater than for the wild-type
D259A
-
specific activity with propionaldehyde as substrate is 2.3fold greater than for wild-type
D259G
-
specific activity is 2fold greater than for the wild-type
D259G
-
specific activity with propionaldehyde as substrate is 1.7fold greater than for wild-type
D469T
-
specific activity with propionaldehyde as substrate is 4.9fold greater than for wild-type. 8.5fold improvement in specificity towards propionaldehyde relative to glycolaldehyde
D469T
-
formation of (3S)-1,3-dihydroxypentan-2-one in 64% enantiomeric excess in the reaction of propanal + beta-hydroxypyruvate
D469T
-
the mutant shows higher activity with 3-formylbenzoic acid and 4-formylbenzoic acid compared to the wild type enzyme
D469Y
-
specific activity with propionaldehyde as substrate is 4.4fold greater than for wild-type. 64fold improvement in specificity towards propionaldehyde relative to glycolaldehyde
D469Y
-
formation of (3R)-1,3-dihydroxypentan-2-one in 53% enantiomeric excess in the reaction of propanal + beta-hydroxypyruvate
H461S
-
specific activity is 4.8fold greater than for the wild-type
H461S
-
specific activity with propionaldehyde as substrate is 1.4fold greater than for wild-type
R358I
-
specific activity is 2.1fold greater than for the wild-type
R358I
-
specific activity with propionaldehyde as substrate is 1.9fold greater than for wild-type
R358P
-
specific activity is 1.5fold greater than for the wild-type
R358P
-
specific activity with propionaldehyde as substrate is 1.5fold greater than for wild-type
R520G
-
specific activity is 2.1fold greater than for the wild-type
R520G
-
specific activity with propionaldehyde as substrate is lower than for wild-type
R520P
-
specific activity is 2.3fold greater than for the wild-type
R520P
-
specific activity with propionaldehyde as substrate is lower than for wild-type
R520Stop
-
specific activity is 3.6fold greater than for the wild-type
R520Stop
-
specific activity with propionaldehyde as substrate is lower than for wild-type
R520V
-
specific activity is 3.6fold greater than for the wild-type
R520V
-
specific activity with propionaldehyde as substrate is 4.7fold greater than for wild-type
S188Q
-
specific activity is 2.3fold greater than for the wild-type
S188Q
-
specific activity with propionaldehyde as substrate is lower than for wild-type
additional information
tktA mutants are slightly slower growing on LB medium. TktA tktB double mutant shows growth inhibition in LB medium comparable to that observed in tktA ppGpp null strains. DELTAtktB::kan mutation confers synthetic growth defects in the tktA mutant similar to that observed from ppGpp deficiency. PpGpp regulates transketolase B activity in the tktA relA256 mutant
additional information
tktA mutants are slightly slower growing on LB medium. TktA tktB double mutant shows growth inhibition in LB medium comparable to that observed in tktA ppGpp null strains. DELTAtktB::kan mutation confers synthetic growth defects in the tktA mutant similar to that observed from ppGpp deficiency. PpGpp regulates transketolase B activity in the tktA relA256 mutant
additional information
-
tktA mutants are slightly slower growing on LB medium. TktA tktB double mutant shows growth inhibition in LB medium comparable to that observed in tktA ppGpp null strains. DELTAtktB::kan mutation confers synthetic growth defects in the tktA mutant similar to that observed from ppGpp deficiency. PpGpp regulates transketolase B activity in the tktA relA256 mutant
additional information
-
deletion of tktA increases antibiotic and oxidative stress susceptibilities
additional information
on LB medium, tktB mutants show no growth defect. TktA tktB double mutant shows growth inhibition in LB medium comparable to that observed in tktA ppGpp null strains. DELTAtktB::kan mutation confers synthetic growth defects in the tktA mutant similar to that observed from ppGpp deficiency. PpGpp regulates transketolase B activity in the tktA relA256 mutant
additional information
on LB medium, tktB mutants show no growth defect. TktA tktB double mutant shows growth inhibition in LB medium comparable to that observed in tktA ppGpp null strains. DELTAtktB::kan mutation confers synthetic growth defects in the tktA mutant similar to that observed from ppGpp deficiency. PpGpp regulates transketolase B activity in the tktA relA256 mutant
additional information
-
on LB medium, tktB mutants show no growth defect. TktA tktB double mutant shows growth inhibition in LB medium comparable to that observed in tktA ppGpp null strains. DELTAtktB::kan mutation confers synthetic growth defects in the tktA mutant similar to that observed from ppGpp deficiency. PpGpp regulates transketolase B activity in the tktA relA256 mutant
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biotechnology
improvement of biocatalytic processes using transketolase over prolonged reaction times will need to address the formation of cofactor-associated intermediate state
medicine
-
TktA interacts with MarR. TktA decreases MarR repressor activity. Overexpressing tktA decreases antibiotic susceptibility. Endogenous TktA enhances multiple antibiotic resistance to a small degree through release of MarR repression of the marRAB operon
analysis
-
low cost, rapid colorimetric transketolase assay, able to detect value above 8% bioconversion using non-alpha-hydroxylated aldehydes as acceptor substrates. The assay is significantly faster and more convenient to use than HPLC and can be used with a range of aliphatic and aromatic aldehydes. In addition, analysis of the alpha,alpha'-dihydroxyketone produced in the bioconversion can be quantified using this assay system with high-throughput. Furthermore, this method has the potential to be used to screen other chemical reactions or bioconversions leading to the formation of products possessing a 2-hydroxyketone motif
analysis
-
a rapid microplate-based approach for measuring the denaturation curves by intrinsic tryptophan fluorescence for simple monomeric and two-state unfolding proteins like transketolase
analysis
-
establishment of a rapid microplate-based HPLC assay for transketolase, for rapidly determining substrate and product concentration suitable for optimisation of biocatalytic process conditions and screening directed evolution libraries, which can be used to determine transketolase activity with a throughput of up to 1200 samples per day, whereas the well-to-well variation from HPLC measurement is just 1.9% for the lowest activities measured
analysis
-
highly effective, stable and sensitive method for measuring TKT activity, incorporating xylulokinase, which induces generation of xylulose 5-phosphate from xylulose, from Saccharomyces cerevisiae into conventional TKT assay
analysis
-
tetrazolium red-based colorimetric assay to screen for transketolase activity with a range of aldehyde acceptors. The assay is able to detect >8% bioconversion using non-alpha-hydroxylated aldehydes as acceptor substrates and is significantly faster and more convenient to use than chromatographic procedures
analysis
-
development of a gas chromatography-based method to screen enzyme activity and stereoselectivity on a wide range of polyol substrates. Method shows reproducibility, sensitivity and range of detection. In combination with HPLC screening, it can be used efficiently to test mutant libraries obtained by directed evolution methods
synthesis
-
desing of an enzyme microreaktor by reversible immobilization of His6-tagged enzyme a 200-microm ID fused silica capillary for quantitative kinetic analysis. Transketolase kinetic parameters in the mircoreactor are comparable with those measured in free solution. Quantitative elution of the immobilized transketolase and the regeneration and reuse of the derivatized capillary over five cycles are possible
synthesis
-
mathematical model for the modes of operation in the reaction of beta-hydroxypyruvate and glycolaldehyde as an alternative to a batch process. The performance of the system strongly depends on the solubility of beta-hydroxypyruvate. The best option for the base case scenario is to use an initial beta-hydroxypyruvate concentration at its solubility level with a slight excess of glycolaldehyde and an initial catalyst concentration of 0.5 g/l for 120 min
additional information
ppGpp-dependent functional pathway that operates through transketolase B, and which is buffered in wild-type strain by the presence of an isozyme, transketolase A
additional information
ppGpp-dependent functional pathway that operates through transketolase B, and which is buffered in wild-type strain by the presence of an isozyme, transketolase A
additional information
-
ppGpp-dependent functional pathway that operates through transketolase B, and which is buffered in wild-type strain by the presence of an isozyme, transketolase A
additional information
-
phylogenetically variant active-site residues are useful for modulating activity of transketolase on natural or structurally-homologous substrates, whereas conserved residues which no longer interact with modified target substrates are useful sites to apply saturation mutagenesis for improvement of activity of transketolase
additional information
ppGpp-dependent functional pathway that operates through transketolase B, and which is buffered in wild-type strain by the presence of an isozyme, transketolase A
additional information
ppGpp-dependent functional pathway that operates through transketolase B, and which is buffered in wild-type strain by the presence of an isozyme, transketolase A
additional information
-
ppGpp-dependent functional pathway that operates through transketolase B, and which is buffered in wild-type strain by the presence of an isozyme, transketolase A
additional information
-
strategy for identifying target sites for focussed saturation mutagenesis of transketolase, for the incremental modification of substrate specificity. Shell active-site residues that are phylogenetically variant can be randomly mutated to improve the overall activity but not specificity of transketolase. Residues with low sequence entropy that no longer interact with either of the smaller target substrates can similarly provide non-specific activity improvements in at least half of the mutants. The other half of these mutants show a preference for the hydroxylated substrate. Residues with low sequence entropy that interact directly with altered regions of the target substrate are most likely to improve the substrate specificity
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Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate
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Escherichia coli
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41
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Escherichia coli (P27302)
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41
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Escherichia coli, Homo sapiens
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Transketolase A, an enzyme in central metabolism, derepresses the marRAB multiple antibiotic resistance operon of Escherichia coli by interaction with MarR
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66
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2007
Escherichia coli
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2008
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-
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-
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Process modelling and simulation of a transketolase mediated reaction: Analysis of alternative modes of operation
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47
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-
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26
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155
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100
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Towards a mechanistic understanding of factors controlling the stereoselectivity of transketolase
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10
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-
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Second generation engineering of transketolase for polar aromatic aldehyde substrates
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18
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-
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6
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