2.2.1.1: transketolase
This is an abbreviated version!
For detailed information about transketolase, go to the full flat file.
Word Map on EC 2.2.1.1
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2.2.1.1
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thiamin
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pentose
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erythrocyte
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pyrophosphate
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transaldolase
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glucose-6-phosphate
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tpp
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ribose
-
5-phosphate
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aldolase
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non-oxidative
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glycation
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encephalopathy
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pyridoxine
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apoenzyme
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phosphoglycerate
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wernicke
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baker
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oxythiamine
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neuropathy
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ribose-5-phosphate
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thiamine-deficient
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xylulose
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thiamine-dependent
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6-phosphogluconate
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riboflavin
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calvin
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pharmacology
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drug development
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biotechnology
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pentose-phosphate
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xylulokinase
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industry
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alpha-ketoglutarate
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dihydroxyacetone
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warburg
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phosphoketolase
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3-epimerase
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hemolysates
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pyrophosphokinase
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xylitol
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phosphoribulokinase
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thiaminase
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hydroxypyruvate
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aminopyrimidine
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fructose-6-phosphate
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medicine
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fructose-1,6-bisphosphate
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antivitaminous
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erythrose
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egypt
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thdp-dependent
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diphosphate-dependent
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synthesis
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isotopomer
-
analysis
- 2.2.1.1
- thiamin
- pentose
- erythrocyte
- pyrophosphate
- transaldolase
- glucose-6-phosphate
- tpp
- ribose
- 5-phosphate
- aldolase
-
non-oxidative
-
glycation
- encephalopathy
- pyridoxine
-
apoenzyme
- phosphoglycerate
- wernicke
-
baker
- oxythiamine
- neuropathy
- ribose-5-phosphate
-
thiamine-deficient
- xylulose
-
thiamine-dependent
- 6-phosphogluconate
- riboflavin
-
calvin
- pharmacology
- drug development
- biotechnology
-
pentose-phosphate
- xylulokinase
- industry
- alpha-ketoglutarate
- dihydroxyacetone
-
warburg
- phosphoketolase
-
3-epimerase
- hemolysates
-
pyrophosphokinase
- xylitol
- phosphoribulokinase
- thiaminase
- hydroxypyruvate
- aminopyrimidine
- fructose-6-phosphate
- medicine
- fructose-1,6-bisphosphate
-
antivitaminous
- erythrose
-
egypt
-
thdp-dependent
-
diphosphate-dependent
- synthesis
-
isotopomer
- analysis
Reaction
Synonyms
glycolaldehydetransferase, STM14_2885, STM14_2886, TK16, TKA, TKL, TKL1, Tkl2, TKT, TKT10, TKT3, TKT7, TktA, TktB, TKTc, TKTL-1, TKTL1, TKTL2, TKTp, transketolase, transketolase 10, transketolase 3, transketolase 7, transketolase A, transketolase B, transketolase like 1, transketolase-1, transketolase-like 1, transketolase-like enzyme 1, transketolase-like-1, transketolase-like-1-gene, transketolase-like-2
ECTree
2.2.1.1 transketolaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.2.1.1 - transketolase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A29D
A29E
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
D469S
-
specific activity with propionaldehyde as substrate is lower than for wild-type
D469T
D469T/R520Q
D469Y
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
H100A
-
specific activity with propionaldehyde as substrate is lower than for wild-type
H100F
the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H100I
-
has the same specific activity with propionaldehyde as substrate as the wild-type. Does not improve specific activity towards propionaldehyde
H100L
the mutant shows about 2.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H100V
-
specific activity with propionaldehyde as substrate is lower than for wild-type
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
H26A/H261A
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
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
H461Q
-
specific activity with propionaldehyde as substrate is lower than for wild-type
H461S
H461Y
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
R358P
R358S
the mutant shows about 1.4fold increased activity with L-arabinose compared to the wild type enzyme
R520G
R520I
-
specific activity with propionaldehyde as substrate is lower than for wild-type
R520P
R520Stop
R520V
R520Y
the mutant shows about 2fold increased activity with L-arabinose compared to the wild type enzyme
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
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
D470T
-
the mutant shows slightly increased activity with benzaldehyde compared to the wild type enzyme
D477A
the mutant shows a kcat/KM value decrease for (2R)-hydroxylated aldehydes decrease by three orders of magnitude compared to the wild type enzyme
F435L/D470E
L191I/D470L
-
the mutant has an activity improvement of roughly 7.4fold compared to the wild type enzyme
L191V/D470
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the mutant exhibits high 3R stereoselectivity as compared to the wild type enzyme
L191V/D470I
-
the mutant exhibits 74% 3R stereoselectivity and 5.8fold activity improvement as compared to the wild type enzyme
L191V/D470R
-
the mutant exhibits 84% 3R stereoselectivity as compared to the wild type enzyme
L382D/D470S
L382E/D470T
-
the mutant shows increased activity with benzaldehyde compared to the wild type enzyme
L382F/D470
-
the mutant has specific activity towards propanal 11 times higher than that of the wild type enzyme, with high yield of the 3S product
L382I/D470L
-
the mutant shows inversed stereoselectivity with low yield of the 3R product
L382N/D470S
-
the mutant shows strongly increased activity with benzaldehyde compared to the wild type enzyme
L382N/D470T
-
the mutant shows increased activity with benzaldehyde compared to the wild type enzyme
R433A
-
lower activity than wild-type enzyme, less stable at 55°C than wild-type
D477A
H103A
-
mutantion does not affect affinity of the coenzyme to apoenzyme in presence of Ca2+, but affects all the kinetic parameters for coenzyme-apoenzyme interaction in presence of Mg2+. Acceleration of one-substrate reaction with slow-down of two-substrate reaction, kinetics
H263A
H27A
in the reaction with sedoheptulose 7-phosphate (backward) the mutant exhibits weaker activity relative to the wild type enzyme
R356L
in the reaction with D-xylulose 5-phosphate (forward) the mutant exhibits weaker activity relative to the wild type enzyme
R525L
in the reaction with D-xylulose 5-phosphate (forward) the mutant exhibits weaker activity relative to the wild type enzyme
additional information
A29D
-
specific activity with propionaldehyde as substrate is lower than for wild-type
A29E
-
specific activity with propionaldehyde as substrate is 3.4fold greater than for wild-type
D259A
-
specific activity with propionaldehyde as substrate is 2.3fold greater than for wild-type
D259G
-
specific activity with propionaldehyde as substrate is 1.7fold 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
D469E
the mutant shows about 4.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
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 activities towards the three benzaldehyde analogues, 3-formylbenzoic acid, 4-formylbenzoic acid and 3-hydroxybenzaldehyde compared to the wild type enzyme
D469T
-
the mutant shows higher activity with 3-formylbenzoic acid and 4-formylbenzoic acid compared to the wild type enzyme
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
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
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
H26A
-
specific activity with propionaldehyde as substrate is 2.3fold greater than for wild-type
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
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)
H26Y
-
formation of (3R)-1,3-dihydroxypentan-2-one in 88% enantiomeric excess in the reaction of propanal + beta-hydroxypyruvate
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
H461S
-
specific activity with propionaldehyde as substrate is 1.4fold greater than for wild-type
H461Y
-
specific activity with propionaldehyde as substrate is lower than for wild-type
H461Y
the mutant shows about 1.2fold increased activity with L-arabinose compared to the wild type enzyme
R358I
-
specific activity with propionaldehyde as substrate is 1.9fold greater than for wild-type
R358I
the mutant shows about 1.2fold increased activity with L-arabinose compared to the wild type enzyme
R358P
-
specific activity with propionaldehyde as substrate is 1.5fold greater than for wild-type
R358P
the mutant shows about 1.4fold increased activity with L-arabinose compared to the wild type enzyme
R520G
-
specific activity with propionaldehyde as substrate is lower than for wild-type
R520P
-
specific activity with propionaldehyde as substrate is lower than for wild-type
R520P
the mutant shows about 1.5fold increased activity with L-arabinose compared to the wild type enzyme
R520Stop
-
specific activity with propionaldehyde as substrate is lower than for wild-type
R520V
-
specific activity with propionaldehyde as substrate is 4.7fold greater than for wild-type
S188Q
-
specific activity with propionaldehyde as substrate is lower than for wild-type
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
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
F435L/D470E
-
the mutant shows a large activity improvement (4.9fold) compared to the wild type enzyme
F435L/D470E
-
the mutant shows a roughly 4.9fold activity improvement compared to the wild type enzyme
L382D/D470S
the mutant leads up to 4 and 5fold higher activities towards L-lactaldehyde and L-glyceraldehyde, respectively, compared to the wild type enzyme
L382D/D470S
-
the mutant shows strongly increased activity with benzaldehyde compared to the wild type enzyme
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
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
-
in vitro induction of the expression by arabinose decreases the amount of recombinant enzyme isolated and lowers its specific activity
