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
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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
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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
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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 (KM Value
KM Value on EC 2.2.1.1 - transketolase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
300
L-glyceraldehyde
Km above 300 mM, at pH 7.2 and 50°C
300
L-lactaldehyde
Km above 300 mM, at pH 7.2 and 50°C
1.3
3-formylbenzoic acid
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mutant enzyme S385Y/D469T/R520Q, at pH 7.0 and 22°C
1.7
3-formylbenzoic acid
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mutant enzyme S385T/D469T/R520Q, at pH 7.0 and 22°C
18
3-formylbenzoic acid
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mutant enzyme S385E/D469T/R520Q, at pH 7.0 and 22°C
180
3-Hydroxybenzaldehyde
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mutant enzyme S385T/D469T/R520Q, at pH 7.0 and 22°C
245
3-Hydroxybenzaldehyde
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mutant enzyme S385E/D469T/R520Q, at pH 7.0 and 22°C
390
3-Hydroxybenzaldehyde
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mutant enzyme S385Y/D469T/R520Q, at pH 7.0 and 22°C
2 - 3
4-formylbenzoic acid
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mutant enzyme S385T/D469T/R520Q, at pH 7.0 and 22°C
13
4-formylbenzoic acid
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mutant enzyme S385Y/D469T/R520Q, at pH 7.0 and 22°C
72
4-formylbenzoic acid
-
mutant enzyme S385E/D469T/R520Q, at pH 7.0 and 22°C
0.023
D-erythrose 4-phosphate
A0A0F6B484; A0A0F6B483, A0A0F6B4M5, A0A0F6B6H7
with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.082
D-erythrose 4-phosphate
A0A0F6B484; A0A0F6B483, A0A0F6B4M5, A0A0F6B6H7
with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.099
D-erythrose 4-phosphate
A0A0F6B484; A0A0F6B483, A0A0F6B4M5, A0A0F6B6H7
with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.029
D-fructose 6-phosphate
wild type enzyme, at pH 8.0 and 25°C
0.34
D-fructose 6-phosphate
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pH 7.6, temperature not specified in the publication
0.007
D-ribose 5-phosphate
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and second value 0.698 mM, pH 7.6, presence of 0.1 mM Ca2+, temperature not specified in the publication
0.014
D-ribose 5-phosphate
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pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied, presence of Ca2+
0.058
D-ribose 5-phosphate
A0A0F6B484; A0A0F6B483, A0A0F6B4M5, A0A0F6B6H7
with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.06
D-ribose 5-phosphate
-
pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied
0.08
D-ribose 5-phosphate
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hemiholotransketolase 2, i.e., transketolase, in which the functional active center has a lower affinity for thiamine diphosphate than hemiholotransketolase 1
0.09
D-ribose 5-phosphate
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hemiholotransketolase 1, i. e. transketolase, in which the functional active center has a higher affinity for the coenzyme than the other active center
0.159
D-ribose 5-phosphate
-
pH 7.6, temperature not specified in the publication
0.25
D-ribose 5-phosphate
-
pH 7.6, 25°C, affinity to the second active center when the first center is occupied
0.4
D-ribose 5-phosphate
-
pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied, presence of Mg2+
0.4
D-ribose 5-phosphate
-
pH 7.6, 25°C, affinity to the second active center when the first center is occupied, presence of Mg2+
0.6
D-ribose 5-phosphate
-
pH 7.6, 25°C, affinity to the second active center when the first center is occupied, presence of Ca2+
0.66
D-ribose 5-phosphate
A0A0F6B484; A0A0F6B483, A0A0F6B4M5, A0A0F6B6H7
with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.698
D-ribose 5-phosphate
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and first value 0.007 mM, pH 7.6, presence of 0.1 mM Ca2+, temperature not specified in the publication
0.73
D-ribose 5-phosphate
A0A0F6B484; A0A0F6B483, A0A0F6B4M5, A0A0F6B6H7
with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.021
D-xylulose 5-phosphate
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pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied, presence of Ca2+
0.025
D-xylulose 5-phosphate
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and second value 0.773 mM, pH 7.6, presence of 0.1 mM Ca2+, temperature not specified in the publication
0.04
D-xylulose 5-phosphate
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presence of 1 mM D-ribose 5-phosphate, pH 7.6, temperature not specified in the publication
0.075
D-xylulose 5-phosphate
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pH 7.6, temperature not specified in the publication
0.1
D-xylulose 5-phosphate
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presence of 2 mM D-ribose 5-phosphate, pH 7.6, temperature not specified in the publication
0.115
D-xylulose 5-phosphate
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pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied, presence of Mg2+
0.115
D-xylulose 5-phosphate
-
pH 7.6, 25°C, affinity to the second active center when the first center is occupied, presence of Mg2+
0.12
D-xylulose 5-phosphate
A0A0F6B484; A0A0F6B483, A0A0F6B4M5, A0A0F6B6H7
with excess D-erythrose 4-phosphate as cosubstrate, at pH 7.5 and 37°C
0.145
D-xylulose 5-phosphate
wild type enzyme, with D-erythrose 4-phosphate as cosubstrate, at pH 8.0 and 25°C
0.17
D-xylulose 5-phosphate
A0A0F6B484; A0A0F6B483, A0A0F6B4M5, A0A0F6B6H7
with excess D-erythrose 4-phosphate as cosubstrate, at pH 7.5 and 37°C
0.18
D-xylulose 5-phosphate
A0A0F6B484; A0A0F6B483, A0A0F6B4M5, A0A0F6B6H7
with excess D-erythrose 4-phosphate as cosubstrate, at pH 7.5 and 37°C
0.183
D-xylulose 5-phosphate
wild type enzyme, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C
0.2
D-xylulose 5-phosphate
-
presence of 5 mM D-ribose 5-phosphate, pH 7.6, temperature not specified in the publication
0.232
D-xylulose 5-phosphate
mutant enzyme H27A, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C
0.27
D-xylulose 5-phosphate
A0A0F6B484; A0A0F6B483, A0A0F6B4M5, A0A0F6B6H7
with excess D-ribose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.29
D-xylulose 5-phosphate
A0A0F6B484; A0A0F6B483, A0A0F6B4M5, A0A0F6B6H7
with excess D-ribose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.41
D-xylulose 5-phosphate
-
presence of 10 mM D-ribose 5-phosphate, pH 7.6, temperature not specified in the publication
0.5
D-xylulose 5-phosphate
-
pH 7.6, 25°C, affinity to the second active center when the first center is occupied, presence of Ca2+
0.517
D-xylulose 5-phosphate
mutant enzyme R356L, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C
0.68
D-xylulose 5-phosphate
mutant enzyme R525L, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C
0.75
D-xylulose 5-phosphate
A0A0F6B484; A0A0F6B483, A0A0F6B4M5, A0A0F6B6H7
with excess D-ribose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.773
D-xylulose 5-phosphate
-
and first value 0.025 mM, pH 7.6, presence of 0.1 mM Ca2+, temperature not specified in the publication
55
propionaldehyde
-
mutant D469T, 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
140
propionaldehyde
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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
0.031
sedoheptulose 7-phosphate
wild type enzyme, at pH 8.0 and 25°C
0.294
sedoheptulose 7-phosphate
mutant enzyme H27A, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C
0.0365
Xylulose 5-phosphate
-
KM for the first active center of transketolase in the presence of Ca2+
0.16
Xylulose 5-phosphate
-
KM for the second active center of transketolase in the presence of Ca2+
additional information
additional information
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kinetic data concerning the lag phase of transketolase reaction
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additional information
additional information
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modeling and simulation of the reaction. Among six kinetic parameters that govern the performance of the reaction, the modification of the MichaelisMenten 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
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