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Information on EC 2.2.1.1 - transketolase and Organism(s) Escherichia coli and UniProt Accession P27302

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     2 Transferases
         2.2 Transferring aldehyde or ketonic groups
             2.2.1 Transketolases and transaldolases
                2.2.1.1 transketolase
IUBMB Comments
A thiamine-diphosphate protein. Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO2 and R-CHOH-CO-CH2OH. The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.
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Escherichia coli
UNIPROT: P27302
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
transketolase, tktl1, transketolase a, transketolase-like 1, tktl-1, transketolase-like-1, tktl2, transketolase-like enzyme 1, transketolase-like-2, glycolaldehydetransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycolaldehydetransferase
-
-
-
-
transketolase A
-
-
transketolase B
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
keto group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glycolaldehydetransferase
A thiamine-diphosphate protein. Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO2 and R-CHOH-CO-CH2OH. The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-48-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 pyruvate
erythrulose
show the reaction diagram
-
-
-
?
3-formylbenzoic acid + pyruvate
3-(2-oxopropanoyl)benzoate + CO2
show the reaction diagram
-
-
-
?
3-formylbenzoic acid + pyruvate
3-(2-oxopropanoyl)benzoic acid + CO2
show the reaction diagram
-
-
-
ir
3-hydroxypyruvate + n-pentanal
1,3-dihydroxy-2-heptanone + CO2
show the reaction diagram
3% yield after 1 h (92% (S)), 12% yield after 3 h (87% (S))
-
-
ir
3-hydroxypyruvate + propanal
1,3-dihydroxy-2-pentanone + CO2
show the reaction diagram
12% yield after 1 h (57% (S)), 32% yield after 3 h (53% (S))
-
-
ir
beta-hydroxypyruvate + glycolaldehyde
L-erythrulose + CO2
show the reaction diagram
-
-
-
?
D-erythrose 4-phosphate + D-xylulose 5-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 6-phosphate + D-ribose 5-phosphate
D-erythrose 4-phosphate + sedoheptulose 7-phosphate
show the reaction diagram
-
-
-
?
D-glyceraldehyde 3-phosphate + D-fructose 6-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
show the reaction diagram
-
-
-
?
D-ribose-5-phosphate + L-erythrulose
D-sedoheptulose 7-phosphate + glycolaldehyde
show the reaction diagram
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
glycolaldehyde + pyruvate
3,4-dihydroxy-2-butanone + CO2
show the reaction diagram
-
-
-
?
hexanal + 2-oxoheptanoic acid
7-hydroxydodecan-6-one + CO2
show the reaction diagram
-
-
-
?
hexanal + pyruvate
2-hydroxyheptanal + CO2
show the reaction diagram
-
-
-
?
hydroxypyruvate + D-ribose-5-phosphate
D-sedoheptulose 7-phosphate
show the reaction diagram
-
-
-
ir
hydroxypyruvate + glycolaldehyde
L-erythrulose + ?
show the reaction diagram
-
-
-
?
L-arabinose + lithium beta-hydroxypyruvate
L-gluco-heptulose + CO2 + Li+
show the reaction diagram
48% conversion after 24 h
-
-
?
pentanal + 2-oxohexanoic acid
6-hydroxydecan-5-one + CO2
show the reaction diagram
-
-
-
?
pentanal + pyruvate
2-hydroxyhexanal + CO2
show the reaction diagram
-
-
-
?
propionaldehyde + 2-oxobutanoic acid
4-hydroxyhexan-3-one + CO2
show the reaction diagram
-
-
-
?
propionaldehyde + pyruvate
2-hydroxybutanal + CO2
show the reaction diagram
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
show the reaction diagram
2 propanal + 2 lithium beta-hydroxypyruvate
(3S)-1,3-dihydroxypentan-2-one + (3R)-1,3-dihydroxypentan-2-one + 2 CO2 + 2 Li+
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
3-hydroxybenzaldehyde + hydroxypyruvate
1,3-dihydroxy-1-(3-hydroxyphenyl)propan-2-one + CO2
show the reaction diagram
-
-
-
-
?
4-formylbenzoic acid + hydroxypyruvate
4-(1,3-dihydroxy-2-oxopropyl)benzoic acid + CO2
show the reaction diagram
-
-
-
-
?
beta-hydroxypyruvate + glycolaldehyde
L-erythrulose + CO2
show the reaction diagram
-
-
-
-
?
D-erythrose + ?
?
show the reaction diagram
-
-
-
-
?
D-erythrose 4-phosphate + ?
?
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde 3-phosphate + D-fructose 6-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
show the reaction diagram
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
DL-glyceraldehyde + ?
?
show the reaction diagram
-
-
-
-
?
DL-glyceraldehyde 3-phosphate + ?
?
show the reaction diagram
-
-
-
-
?
formaldehyde + ?
?
show the reaction diagram
-
-
-
-
?
fructose 6-phosphate + ?
?
show the reaction diagram
-
-
-
-
?
glycolaldehyde + ?
?
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + ?
?
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + glycolaldehyde
L-erythrulose + ?
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + ribose 5-phosphate
sedoheptulose 7-phosphate + ?
show the reaction diagram
-
-
-
-
?
Li-hydroxypyruvate + propionaldehyde
1,3-dihydroxypentan-2-one + ?
show the reaction diagram
-
-
-
-
?
lithium beta-hydroxypyruvate + glycolaldehyde
L-erythrulose + ?
show the reaction diagram
-
-
-
-
?
propanal + glycolaldehyde
(3S)-1,3-dihydroxypentan-2-one
show the reaction diagram
-
-
-
-
?
sedoheptulose 7-phosphate + ?
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
show the reaction diagram
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
thiamine diphosphate
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
bound at the subunit interface
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Urea
denaturation of holo-transketolase by urea displays at least three transitions, where only the final equilibrium denaturation transition is the same for both apo-transketolase and holo-transketolase. Enzyme is deactivated initially by changes in structure associated with the cofactors, but this event does not release the cofactor from the enzyme. Holo-transketolase does not denature to apo-transketolase at 2 M urea. Complete dissociation of cofactors from holo-transketolase at 3.8 M urea without formation of the compact form of apo-transketolase (intermediate form). Holo-transketolase and apo-transketolase at 7.2 M urea both show a common denatured form
3-formylbenzoic acid
-
substrate inhibition
D-arabinose 5-phosphate
-
competitive inhibition
L-erythrulose
-
competitive inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hydrogen peroxide
-
oxidative stress increases tktA expression. Induces tktA at 1 h treatment, while an increase in marRAB operon expression occurs only after 3 h exposure
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3 - 56
3-formylbenzoic acid
180 - 390
3-Hydroxybenzaldehyde
2 - 251
4-formylbenzoic acid
10
D,L-glyceraldehyde
-
-
2.1
D,L-glyceraldehyde 3-phosphate
-
-
150
D-erythrose
-
-
0.09
D-erythrose 4-phosphate
-
-
1.4
D-ribose 5-phosphate
-
-
0.16
D-xylulose 5-phosphate
-
-
31
formaldehyde
-
-
1.1
fructose 6-phosphate
-
-
14 - 200
glycolaldehyde
5.3 - 18
Hydroxypyruvate
26
lithium beta-hydroxypyruvate
-
pH 7.0, 25°C
55 - 140
propionaldehyde
4
sedoheptulose 7-phosphate
-
-
additional information
additional information
-
modeling and simulation of the reaction. Among six kinetic parameters that govern the performance of the reaction, the modification of the Michaelis–Menten constant for glycolaldehyde, inhibition constant for beta-hydroxypyruvate and the rate of reaction result in a positive effect on the performance of the reaction. An increase of inhibition constant for beta-hydroxypyruvate by 10fold yields a 35% increase in the level of achieved conversion. A 10fold decrease in Michaelis-Menten constant for glycolaldehyde has similar results, 36%. A 10fold increase of the rate of reaction results in almost 150% increase in the achievable product concentration
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6 - 34
3-formylbenzoic acid
0.6 - 2.1
3-Hydroxybenzaldehyde
0.2 - 5
4-formylbenzoic acid
410000
lithium beta-hydroxypyruvate
-
pH 7.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.24 - 5.4
3-formylbenzoic acid
0.0024 - 0.0055
3-Hydroxybenzaldehyde
0.0046 - 0.11
4-formylbenzoic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
-
in phosphate buffer
8 - 8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 11
-
more than 50% of maximum activity
6 - 8
-
more than 80% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
Overexpression or deletion of the enzyme gene interferes with MarR repression of the marRAB operon. Deletion of enzyme gene increases antibiotic and oxidative stress susceptibilities, while its overexpression decreases them
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
145000
-
gel filtration
70000
-
2 * 70000
73000
-
alpha2, 2 * 73000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
alpha2, 2 * 73000, SDS-PAGE
homodimer
-
2 * 70000
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, transketolase in a covalent complex with donor ketoses D-xylulose 5-phosphate and D-fructose 6-phosphate at 1.47 A and 1.65 A resolution, reveal significant strain in the tetrahedral cofactor-sugar adducts with a 25-30° out-of-plane distortion of the C2-Calpha bond connecting the carbonyl of the substrates with the C2 of the cofactor’s thiazolium part. The noncovalent complex with acceptor aldose ribose 5-phosphate reveals that the sugar is present in multiple forms, in a strained ring-closed beta-D-furanose form in C2-exo conformation as well as in an extended acyclic aldehyde form, with the reactive C1 aldo function held close to Calpha of the presumably planar carbanion/enamine intermediate
mutant S385Y/D469T/R520Q, hanging drop vapor diffusion method, using 17-22% (w/v) PEG 6000, 2% (v/v) glycerol, 50 mM glycyl-glycine buffer, pH 7.9
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
H26A/H261A
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
D259A
D259G
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
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
D469Y
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
H461S
H461Y
-
specific activity with propionaldehyde as substrate is lower than for wild-type
R358I
R358P
R520G
R520I
-
specific activity with propionaldehyde as substrate is lower than for wild-type
R520P
R520Stop
R520V
S188Q
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
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
complete inactivation
720083
9
-
high pH results in the formation of a native-like state that is only partially inactive. The apo-enzyme structure content also increases at pH 9 to converge on that of the holo-enzyme
720083
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58.3
-
sharp transition in circular dichroism spectra, with appearance of aggregates
60
-
initial inactivation is slow with a first order rate constant of 0.007 per min, but after a lag phase a more rapid inactivation begins with a first order rate constant of 0.023 per min
65
-
inactivation follows single-exponential first-order kinetics with a rate constant of 0.181 per min
additional information
-
10% non-cooperative loss of secondary structure as the temperature increases from 5°C to 50°C. This partial unfolding at moderately elevated temperatures may belinked to the enzyme activation observed at up to 55°C prior to the activity loss at higher temperatures. At 40-55°C the residual activity increases with incubation time and temperature when measured after re-cooling samples to 25°C, indicating that the protein undergoes an irreversible annealing, such that inactive forms of the enzyme are physically altered or activated by temperature
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 250 mM Tris-HCl buffer, pH 7.5, 2 weeks
4°C, 250 mM Tris-HCl buffer, pH 7.5, 2 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged wild-type transketolase purified on Ni-NTA resin
Ni-NTA column chromatography
on Ni-NTA resin
-
on Ni-NTA resin-bound MarR
-
wild-type and mutant A29E purified on Ni-NTA resin
-
wild-type and mutant D469T
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta(DE3) cells
His-tagged wild-type transketolase overexpressed from Escherichia coli XL10-Gold, containing plasmid pQR791
plasmid pGSJ427 carrying the gene for TKA/His6-tag expressed in Escherichia coli strain JM109
construction of plasmid pHR30 using pQE80L vector for IPTG inducible TktB expression
expressed from the self-promoting tktA gene in the plasmid pQR711 in Escherichia coli TOP10 or XL10 cells. Both wild-type and mutant D469T overexpressed from pQR412
-
expression in Escherichia coli
-
expression in Escherichia coli, His-taggged protein
-
into plasmid pQR711 and expressed in Escherichia coli strains BL21-Gold(DE3), JM107, JM109 and XL10-Gold
-
into vector pET21b, tktA overexpressed using the high-copy-number expression plasmid pSPOK in Escherichia coli SPC105
-
overexpression in Escherichia coli
-
tktA gene as His-tagged version complete with its own promotor overexpressed from vector pQR791 in Escherichia coli XL10-Gold
-
tkta gene complete with its natural promoter on the pQR711 plasmid expressed in Escherichia coli TOP10 or XL10 cells. A29E mutation introduced into the pQR412 vector, in which the transketolase gene has an N-terminal His×6 tag. Both wild-type and mutant A29E overexpressed from pQR412
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
hydrogen peroxide induces enzyme expression at 1 h treatment, while an increase in expression of the marRAB operon occurrs only after 3 h exposure and is dependent on the presence of the enzmye gene
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
improvement of biocatalytic processes using transketolase over prolonged reaction times will need to address the formation of cofactor-associated intermediate state
analysis
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
synthesis
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sprenger, G.A.; Schoerken, U.; Sprenger, G.; Sahm, H.
Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains
Eur. J. Biochem.
230
525-532
1995
Escherichia coli
Manually annotated by BRENDA team
Gyamerah, M.; Willetts, A.J.
Kinetics of overexpressed transketolase from Escherichia coli JM 107/pQR 700
Enzyme Microb. Technol.
20
127-134
1997
Escherichia coli
-
Manually annotated by BRENDA team
Schneider, G.; Lindqvist, Y.
Crystallography and mutagenesis of transketolase: mechanistic implications for enzymic thiamin catalysis
Biochim. Biophys. Acta
1385
387-398
1998
Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
Schenk, G.; Duggleby, R.G.; Nixon, P.F.
Properties and functions of the thiamin diphosphate dependent enzyme transketolase
Int. J. Biochem. Cell Biol.
30
1297-1318
1998
Cyberlindnera jadinii, Oryctolagus cuniculus, Escherichia coli, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces pastorianus, Spinacia oleracea, Sus scrofa, Saccharomyces cerevisiae (P23254), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Smith, M.E.; Kaulmann, U.; Ward, J.M.; Hailes, H.C.
A colorimetric assay for screening transketolase activity
Bioorg. Med. Chem.
14
7062-7065
2006
Escherichia coli
Manually annotated by BRENDA team
Lee, J.Y.; Cheong, D.E.; Kim, G.J.
A novel assay system for the measurement of transketolase activity using xylulokinase from Saccharomyces cerevisiae
Biotechnol. Lett.
30
899-904
2008
Escherichia coli
Manually annotated by BRENDA team
Asztalos, P.; Parthier, C.; Golbik, R.; Kleinschmidt, M.; Huebner, G.; Weiss, M.S.; Friedemann, R.; Wille, G.; Tittmann, K.
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
Biochemistry
46
12037-12052
2007
Escherichia coli (P27302), Escherichia coli
Manually annotated by BRENDA team
Aucamp, J.P.; Martinez-Torres, R.J.; Hibbert, E.G.; Dalby, P.A.
A microplate-based evaluation of complex denaturation pathways: structural stability of Escherichia coli transketolase
Biotechnol. Bioeng.
99
1303-1310
2008
Escherichia coli
Manually annotated by BRENDA team
Miller, O.J.; Hibbert, E.G.; Ingram, C.U.; Lye, G.J.; Dalby, P.A.
Optimisation and evaluation of a generic microplate-based HPLC screen for transketolase activity
Biotechnol. Lett.
29
1759-1770
2007
Escherichia coli
Manually annotated by BRENDA team
Martinez-Torres, R.J.; Aucamp, J.P.; George, R.; Dalby, P.A.
Structural stability of E. coli transketolase to urea denaturation
Enzyme Microb. Technol.
41
653-662
2007
Escherichia coli (P27302)
-
Manually annotated by BRENDA team
Alexander-Kaufman, K.; Harper, C.
Transketolase: Observations in alcohol-related brain damage research
Int. J. Biochem. Cell Biol.
41
717-720
2009
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Hibbert, E.G.; Senussi, T.; Costelloe, S.J.; Lei, W.; Smith, M.E.; Ward, J.M.; Hailes, H.C.; Dalby, P.A.
Directed evolution of transketolase activity on non-phosphorylated substrates
J. Biotechnol.
131
425-432
2007
Escherichia coli
Manually annotated by BRENDA team
Hibbert, E.G.; Senussi, T.; Smith, M.E.; Costelloe, S.J.; Ward, J.M.; Hailes, H.C.; Dalby, P.A.
Directed evolution of transketolase substrate specificity towards an aliphatic aldehyde
J. Biotechnol.
134
240-245
2008
Escherichia coli
Manually annotated by BRENDA team
Domain, F.; Bina, X.R.; Levy, S.B.
Transketolase A, an enzyme in central metabolism, derepresses the marRAB multiple antibiotic resistance operon of Escherichia coli by interaction with MarR
Mol. Microbiol.
66
383-394
2007
Escherichia coli
Manually annotated by BRENDA team
Harinarayanan, R.; Murphy, H.; Cashel, M.
Synthetic growth phenotypes of Escherichia coli lacking ppGpp and transketolase A (tktA) are due to ppGpp-mediated transcriptional regulation of tktB
Mol. Microbiol.
69
882-894
2008
Escherichia coli (P27302), Escherichia coli (P33570), Escherichia coli
Manually annotated by BRENDA team
Smith, M.; Hibbert, E.; Jones, A.; Dalby, P.; Hailesa, H.
Enhancing and reversing the stereoselectivity of Escherichia coli transketolase via single-point mutations
Adv. Synth. Catal.
350
2631-2638
2008
Escherichia coli
-
Manually annotated by BRENDA team
Sayar, N.; Chen, B.; Lye, G.; Woodley, J.
Modelling and simulation of a transketolase mediated reaction: Sensitivity analysis of kinetic parameters
Biochem. Eng. J.
47
1-9
2009
Escherichia coli
-
Manually annotated by BRENDA team
Sayar, N.; Chen, B.; Lye, G.; Woodley, J.
Process modelling and simulation of a transketolase mediated reaction: Analysis of alternative modes of operation
Biochem. Eng. J.
47
10-18
2009
Escherichia coli
-
Manually annotated by BRENDA team
Matosevic, S.; Lye, G.J.; Baganz, F.
Design and characterization of a prototype enzyme microreactor: Quantification of immobilized transketolase kinetics
Biotechnol. Prog.
26
118-126
2009
Escherichia coli
Manually annotated by BRENDA team
Jahromi, R.R.; Morris, P.; Martinez-Torres, R.J.; Dalby, P.A.
Structural stability of E. coli transketolase to temperature and pH denaturation
J. Biotechnol.
155
209-216
2011
Escherichia coli
Manually annotated by BRENDA team
Domain, F.; Bina, X.; Levy, S.
Transketolase A, an enzyme in central metabolism, derepresses the marRAB multiple antibiotic resistance operon of Escherichia coli by interaction with MarR
Mol. Microbiol.
80
853-853
2011
Escherichia coli
Manually annotated by BRENDA team
Ranoux, A.; Arends, I.; Hanefeld, U.
Development of screening methods for transketolase activity and substrate scope
Tetrahedron Lett.
53
790-793
2012
Saccharomyces cerevisiae, Escherichia coli
-
Manually annotated by BRENDA team
Vimala, A.; Harinarayanan, R.
Transketolase activity modulates glycerol-3-phosphate levels in Escherichia coli
Mol. Microbiol.
100
263-277
2016
Escherichia coli, Escherichia coli AV139
Manually annotated by BRENDA team
Baierl, A.; Theorell, A.; Mackfeld, U.; Marquardt, P.; Hoffmann, F.; Moers, S.; Noeh, K.; Buchholz, P.; Pleiss, J.; Pohl, M.
Towards a mechanistic understanding of factors controlling the stereoselectivity of transketolase
ChemCatChem
10
2601-2611
2018
Escherichia coli (P27302)
-
Manually annotated by BRENDA team
Payongsri, P.; Steadman, D.; Hailes, H.C.; Dalby, P.A.
Second generation engineering of transketolase for polar aromatic aldehyde substrates
Enzyme Microb. Technol.
71
45-52
2015
Escherichia coli
Manually annotated by BRENDA team
Yu, H.; Hernandez Lopez, R.I.; Steadman, D.; Mendez-Sanchez, D.; Higson, S.; Cazares-Koerner, A.; Sheppard, T.D.; Ward, J.M.; Hailes, H.C.; Dalby, P.A.
Engineering transketolase to accept both unnatural donor and acceptor substrates and produce alpha-hydroxyketones
FEBS J.
287
1758-1776
2020
Escherichia coli (P27302)
Manually annotated by BRENDA team
Subrizi, F.; Cardenas-Fernandez, M.; Lye, G.; Ward, J.; Dalby, P.; Sheppard, T.; Hailes, H.
Transketolase catalysed upgrading of L-arabinose The one-step stereoselective synthesis of L-gluco-heptulose
Green Chem.
18
3158-3165
2016
Escherichia coli (P27302)
-
Manually annotated by BRENDA team
Klaus, A.; Pfirrmann, T.; Glomb, M.A.
Transketolase A from E. coli significantly suppresses protein glycation by glycolaldehyde and glyoxal in vitro
J. Agric. Food Chem.
65
8196-8202
2017
Escherichia coli (P27302), Escherichia coli
Manually annotated by BRENDA team
Affaticati, P.E.; Dai, S.B.; Payongsri, P.; Hailes, H.C.; Tittmann, K.; Dalby, P.A.
Structural analysis of an evolved transketolase reveals divergent binding modes
Sci. Rep.
6
35716
2016
Escherichia coli (P27302), Escherichia coli
Manually annotated by BRENDA team