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Information on EC 2.2.1.1 - transketolase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P23254
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2.2.1.1 transketolaseIUBMB 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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Word Map
- 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
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
transketolase, tktl1, transketolase a, transketolase-like 1, tktl-1, transketolase-like-1, tktl2, transketolase-like enzyme 1, transketolase-like-2, glycolaldehydetransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycolaldehydetransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
donor substrate, but not acceptor substrate, enhances affinity of cofactor to apoenzyme to a different degree for the two active centers, resulting in a negative cooperativity for cofactor binding. Reaction intermediate is a 2-(alpha,beta-dihydroxyethyl)-thiamine diphosphate, which exhibits a higher affinity for the enzyme than thiamine diphosphate
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
H103 stabilizes reaction intermediate, kinetics
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+, caused by increase in the rate of conformational transfer after the thiamine diphosphate binding completion in both active centers, kinetic analysis
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
keto group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -
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
9014-48-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
glyceraldehyde 3-phosphate + D-glyceraldehyde 3-phosphate
D-xylulose 5-phosphate + D-xylulose 5-phosphate
-
-
-
r
hydroxypyruvate + ribose 5-phosphate
sedoheptulose 7-phosphate + ?
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
D-fructose 6-phosphate + Fe(CN)3-
glycolic acid + D-erythrose 4-phosphate + Fe(CN)64- + H+
-
-
-
-
?
D-ribose 5-phosphate + 2,3-dihydroxy-4-O-(2'-oxo-benzopyran-7'-yl)-D-threose
?
-
fluorogenic substrate as probe for measuring wild-type or altered transketolase activity from variants with improved or new properties acquired by random mutagenesis
-
-
?
D-ribose 5-phosphate + 7'-(2,3,5-trihydroxy-4-oxo-pentyl)oxycoumarin
?
-
fluorogenic substrate as probe for measuring wild-type or altered transketolase activity from variants with improved or new properties acquired by random mutagenesis
-
-
?
D-ribose 5-phosphate + 7-(2',3',5'-trihydroxy-4'-oxo-pentyl)oxycoumarine
?
-
fluorogenic substrate as probe for measuring wild-type or altered transketolase activity from variants with improved or new properties acquired by random mutagenesis
-
-
?
D-ribose 5-phosphate + D-xylulose 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
hydroxypyruvate + ferricyanide + H2O
glycolic acid + ferrocyanide + ?
-
-
-
-
?
hydroxypyruvate + ribose 5-phosphate
sedoheptulose 7-phosphate + ?
-
-
-
-
?
N-acetyl-O'-(2R,3S,5-trihydroxy-4-oxopentyl)-L-tyrosine ethyl ester + D-ribose 5-phosphate
N-acetyl-O-[(2R)-2-hydroxy-3-oxopropyl]-L-tyrosine + D-sedoheptulose 7-phosphate
-
transketolase catalyzes the hydroxyacetyl group transfer from the donor substrate N-acetyl-O'-(2R,3S,5-trihydroxy-4-oxopentyl)-L-tyrosine ethyl ester to D-ribose-5-phosphate, the natural acceptor substrate of transketolase. Transketolase catalyzes C2-C3 bond cleavage from N-acetyl-O'-(2R,3S,5-trihydroxy-4-oxopentyl)-L-tyrosine ethyl ester
-
-
?
ribulose 5-phosphate + ribose 5-phosphate
a heptulose phosphate + glyceraldehyde 3-phosphate
-
ribulose is cleaved and ribose acts as acceptor
-
-
?
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
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
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
-
L-erythrulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-arabinose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-deoxyribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
glycolaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
DL-glyceraldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
and acceptor substrates may be: D-glyceraldehyde 3-phosphate
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
and acceptor substrates may be: D-glyceraldehyde 3-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
octulose 8-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
allose 6-phosphate, glucose 6-phosphate, formaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-ribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-erythrose 4-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
sedoheptulose 7-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
wide specificity for both reactants: donor substrates may be: fructose 6-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-xylulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ubiquitous enzyme, involved in carbohydrate and nucleic acid metabolism, bacterial pentose biosynthesis, microbial shikimic acid biosynthesis, formaldehyde metabolism
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
pathway in non-oxidative sequence of pentose cycle
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
two optical methods for transketolase activity assay using only one substrate, xylulose 5-phosphate or glycol aldehyde. For transketolase activity assay in the first method, it is necessary to add auxiliary enzyme, glyceraldehyde phosphate dehydrogenase. It is not needed in the second method. The range of transketolase concentration in the activity assay is 0.036-0.144 U/ml for the first method and 1.8-6.8 U/ml for the second one
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
in presence of Ca2+, the active centers of the enzyme are nonequivalent with respect to both ribose 5-phosphate and xylulose 5-phosphate binding
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
the active centers of the enzyme are nonequivalent with respect to ribose 5-phosphate binding. Under the conditions where only one out of the two active centers of transketolase is functional, their affinities for ribose 5-phosphate are identical. Nonequivalence becomes apparent when the substrate interacts with one of the two active centers. As a consequence, the affinity of the second active center for ribose 5-phosphate decreases
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
-
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
-
-
-
ir
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
enantioselective
-
-
?
additional information
?
-
the enzyme shows a broad substrate specificity with D-xylulose 5-phosphate, D-fructose 6-phosphate, erythrulose 4-phosphate, and sedoheptulose 7-phosphate as typical donor substrates as well as D-ribose 5-phosphate, glyceraldehyde 3-phosphate, and D-erythrose 4-phosphate as typical acceptor substrates
-
-
?
additional information
?
-
-
the enzyme shows a broad substrate specificity with D-xylulose 5-phosphate, D-fructose 6-phosphate, erythrulose 4-phosphate, and sedoheptulose 7-phosphate as typical donor substrates as well as D-ribose 5-phosphate, glyceraldehyde 3-phosphate, and D-erythrose 4-phosphate as typical acceptor substrates
-
-
?
additional information
?
-
-
no acceptors are D-ribose, formaldehyde, acetaldehyde, glucose 6-phosphate
-
-
?
additional information
?
-
-
transketolase reaction is irreversible when hydroxypyruvate is used as a donor substrate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
r
glyceraldehyde 3-phosphate + D-glyceraldehyde 3-phosphate
D-xylulose 5-phosphate + D-xylulose 5-phosphate
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
D-ribose 5-phosphate + D-xylulose 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
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
r
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
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ubiquitous enzyme, involved in carbohydrate and nucleic acid metabolism, bacterial pentose biosynthesis, microbial shikimic acid biosynthesis, formaldehyde metabolism
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
pathway in non-oxidative sequence of pentose cycle
-
-
?
additional information
?
-
the enzyme shows a broad substrate specificity with D-xylulose 5-phosphate, D-fructose 6-phosphate, erythrulose 4-phosphate, and sedoheptulose 7-phosphate as typical donor substrates as well as D-ribose 5-phosphate, glyceraldehyde 3-phosphate, and D-erythrose 4-phosphate as typical acceptor substrates
-
-
?
additional information
?
-
-
the enzyme shows a broad substrate specificity with D-xylulose 5-phosphate, D-fructose 6-phosphate, erythrulose 4-phosphate, and sedoheptulose 7-phosphate as typical donor substrates as well as D-ribose 5-phosphate, glyceraldehyde 3-phosphate, and D-erythrose 4-phosphate as typical acceptor substrates
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
as opposed to the kinetically stabilized carbanion/enamine intermediate in transketolase when reconstituted with the native cofactor, 2-(1,2-dihydroxyethyl)-4'-monomethylaminothiamin diphosphate is rapidly released from the active centers during turnover and accumulates in the medium on a preparative scale
-
thiamine diphosphate
-
-
thiamine diphosphate
-
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
thiamine diphosphate
-
application of a theoretical model of interactions between ligand-binding sites in a dimeric protein for the analysis of thiamine diphosphate binding to yeast transketolase
thiamine diphosphate
-
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate
thiamine diphosphate
-
interaction with the coenzyme binding site of the enzyme is described
thiamine diphosphate
-
theoretical analysis of interaction between thiamine diphosphate-binding sites of transketolase and determination of equilibrium and kinetic constants of individual stages of the interaction between thiamine diphosphate and the apoenzyme in the presence of Ca2+
thiamine diphosphate
-
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate
-
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme
thiamine diphosphate
-
in the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Ca2+
-
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+. Influence of Mg2+ is less pronounced than of Ca2+
Ca2+
-
holoenzyme reconstituted in the presence of Ca2+ is more stable than its Mg2+ counterpart
Ca2+
-
thiamine diphosphate affinity to the enzymes active sites is higher in the presence of Ca2+ than in the presence of Mg2+
Ca2+
-
when Ca2+ is substituted for Mg2+, the two active centers of transketolase are nonequivalent in the ability to bind xylulose 5-phosphate
Ca2+
-
in the presence of Ca2+, the enzyme exhibits strong negative active site cooperativity in both xylulose 5-phosphate binding and ribose 5-phosphate binding and positive cooperativity in the catalytic activity
Ca2+
-
in the presence of free Ca2+, the equivalence of the two active centers of the enzyme is lost. Negative cooperativity is induced on binding of either xylulose 5-phosphate or ribose 5-phosphate, whereupon the catalytic conversion of the bound substrates causes the interaction between the centers to become positively cooperative. Enzyme total activity increases in presence of Ca2+
Mg2+
-
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+. Influence of Mg2+ is less pronounced than of Ca2+
Mg2+
-
holoenzyme reconstituted in the presence of Ca2+ is more stable than its Mg2+ counterpart
Mg2+
-
in the presence of Mg2+, the two active centers of transketolase are equivalent in the ability to bind xylulose 5-phosphate
Mg2+
-
thiamine diphosphate affinity to the enzymes active sites is higher in the presence of Ca2+ than in the presence of Mg2+
Mg2+
-
nonequivalence of the active sites is not observed in presence of Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-ribose 5-phosphate
exerts a time-dependent inhibiting action on enzyme activity in the presence of NaCNBH3
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
active centers of the enzyme are functionally nonequivalent with respect to ribose 5-phosphate binding
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic data concerning the lag phase of transketolase reaction
-
0.007
D-ribose 5-phosphate
-
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
-
pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied, presence of Ca2+
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
-
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
-
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+
0.698
D-ribose 5-phosphate
-
and first value 0.007 mM, pH 7.6, presence of 0.1 mM Ca2+, temperature not specified in the publication
0.021
D-xylulose 5-phosphate
-
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
-
and second value 0.773 mM, pH 7.6, presence of 0.1 mM Ca2+, temperature not specified in the publication
0.075
D-xylulose 5-phosphate
-
pH 7.6, temperature not specified in the publication
0.115
D-xylulose 5-phosphate
-
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+
0.5
D-xylulose 5-phosphate
-
pH 7.6, 25°C, affinity to the second active center when the first center is occupied, presence of Ca2+
0.773
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
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+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
D-xylulose 5-phosphate
-
mutant E418A, cofactor thiamine diphosphate, 25°C, pH 7.6
0.63
D-xylulose 5-phosphate
-
wild-type, cofactor 4-methylamino-thiamine diphosphate, 25°C, pH 7.6
1.8
D-xylulose 5-phosphate
-
mutant E418A, cofactor N1-methyl-thiamine diphosphate, 25°C, pH 7.6
5
D-xylulose 5-phosphate
-
wild-type, cofactor N1-methyl-thiamine diphosphate, 25°C, pH 7.6
45
D-xylulose 5-phosphate
-
wild-type, cofactor thiamine diphosphate, 25°C, pH 7.6
0.002
Hydroxypyruvate
-
mutant E418A, cofactor N1-methyl-thiamine diphosphate, 25°C, pH 7.6
0.005
Hydroxypyruvate
-
wild-type, cofactor N1-methyl-thiamine diphosphate, 25°C, pH 7.6
2.5
Hydroxypyruvate
-
wild-type, cofactor 4-methylamino-thiamine diphosphate, 25°C, pH 7.6
44.5
Hydroxypyruvate
-
wild-type, cofactor thiamine diphosphate, 25°C, pH 7.6
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
gene disruption mutant displays a significant decrease in both growth on xylose and xylose-fermenting ability, and enzmye is also required for utilization of glucose. The rate of xylose consumption and ethanol production is slightly impaired in overexpressing strains
physiological function
growth on xylose and xylose-fermenting ability are slightly influenced in a gene deltion mutant when xylose is used as the sole carbon source. The rate of xylose consumption and ethanol production is slightly impaired in overexpressing strains
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
-
at sufficiently low concentration the apo-, not the holoenzyme dissociates reversibly into 2 subunits of equal molecular weight, individual subunits are equally catalytically active
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cocrystallization of apotransketolase with 5 mM thiamine diphosphate, 5 mM CaCl2, 50 mM fructose-6-phosphate, 13-16% (w/W) polyethylenglycol 6000 in 50 mM glycyl-glycine buffer, pH 7.6, 0.0075 ml of a 20 mg/ml solution mixed with the same amount of mother liquid, space group: P212121
wild-type and mutant E418A in complex with N1-methyl-thiamine diphosphate and wild-type in complex with 4-methylamino-thiamine diphosphate, topology of active sites remains unchanged by cofactor analogues
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme is more stable in presence of Ca2+ than Mg2+. Thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
holoenzyme reconstituted in the presence of Ca2+ is more stable than its Mg2+ counterpart
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, crystalline, several weeks in 0.008 M glycylglycine buffer, pH 7.6
-
2°C, crystalline, several months, after 10 months and longer the enzyme loses its solubility without losing activity
-
prolonged storage of 10 months and longer leads to loss of solubility without loss of activity
-
room temperature, crystalline, in alkaline ammonium sulfate suspension
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of is up-regulated in the presence of xylose
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. In the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
biotechnology
-
substrate specificity of transketolase for the donor substrate is broader than expected. Possibility of detecting wild-type transketolase activity in vitro from a L-tyrosine derivative bearing a D-threo ketose, based on the release of L-tyrosine. For cells both auxotrophic for L-tyrosine and expressing transketolase, it shall be possible to carry out this assay in vivo. This strategy may offer the first stereospecific selection test for transketolase mutants
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Racker, E.
Transketolase
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
5
397-406
1961
Saccharomyces cerevisiae, Cyberlindnera jadinii, Oryctolagus cuniculus, Lactiplantibacillus pentosus, Saccharomyces pastorianus, Spinacia oleracea
-
De La Haba, G.; Leder, I.G.; Racker, E.
Crystalline transketolase from bakers yeast: isolation and properties
J. Biol. Chem.
214
409-426
1955
Saccharomyces cerevisiae
Kochetov, G.A.; Philippov, P.P.; Razjivin, A.P.; Tikhomirova, N.K.
Kinetics of reconstruction of holo-transketolase
FEBS Lett.
53
211-212
1975
Saccharomyces cerevisiae
Kochetov, G.A.
Determination of transketolase activity via ferricyanide reduction
Methods Enzymol.
89
43-44
1982
Saccharomyces cerevisiae
Egan, R.M.; Sable, H.Z.
Transketolase kinetics. The slow reconstitution of the holoenzyme is due to rate-limiting dimerization of the subunits
J. Biol. Chem.
256
4877-4883
1981
Saccharomyces cerevisiae
Demuynck, C.; Fisson, F.; Bennani-Baiti, I.; Samaki, H.; Mani, J.C.
Immunoaffinity purification of transketolases from yeast and spnich leaves
Agric. Biol. Chem.
54
3073-3078
1990
Saccharomyces cerevisiae, Spinacia oleracea
-
Kochetov, G.A.
Transketolase from yeast, rat liver, and pig liver
Methods Enzymol.
90
209-223
1982
Saccharomyces cerevisiae, Rattus norvegicus, Sus scrofa
Kuimov, A.N.; Kovina, M.V.; Kochetov, G.A.
Inhibition of transketolase by N-acetylimidazole
Biochem. Int.
17
517-521
1989
Saccharomyces cerevisiae
Meshalkina, L.E.; Neef, H.; Tjaglo, M.V.; Schellenberger, A.; Kochetov, G.A.
The presence of a hydroxyl group at the C-1 atom of the transketolase substrate molecule is necessary for the enzyme to perform the transferase reaction
FEBS Lett.
375
220-222
1995
Saccharomyces cerevisiae
Nilsson, U.; Meshalkina, L.; Lindqvist, Y.; Schneider, G.
Examination of substrate binding in thiamin diphosphate-dependent transketolase by protein crystallography and site-directed mutagenesis
J. Biol. Chem.
272
1864-1869
1997
Saccharomyces cerevisiae (P23254), Saccharomyces cerevisiae
Wikner, C.; Nilsson, U.; Meshalkina, L.; Udekwu, C.; Lindqvist, Y.; Schneider, G.
Identification of catalytically important residues in yeast transketolase
Biochemistry
36
15643-15649
1997
Saccharomyces cerevisiae
Nilsson, U.; Hecquet, L.; Gefflaut, T.; Guerard, C.; Schneider, G.
Asp477 is a determinant of the enantioselectivity in yeast transketolase
FEBS Lett.
424
49-52
1998
Saccharomyces cerevisiae
Kovina, M.V.; Tikhonova, O.V.; Solov'eva, O.N.; Bykova, I.A.; Ivanov, A.S.; Kochetov, G.A.
Influence of transketolase substrates on its conformation
Biochem. Biophys. Res. Commun.
275
968-972
2000
Saccharomyces cerevisiae (P23254)
Fiedler, E.; Golbik, R.; Schneider, G.; Tittmann, K.; Neef, H.; Konig, S.; Hubner, G.
Examination of donor substrate conversion in yeast transketolase
J. Biol. Chem.
276
16051-16058
2001
Saccharomyces cerevisiae
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
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
Esakova, O.A.; Meshalkina, L.E.; Golbik, R.; Hubner, G.; Kochetov, G.A.
Donor substrate regulation of transketolase
Eur. J. Biochem.
271
4189-4194
2004
Saccharomyces cerevisiae
Golbik, R.; Meshalkina, L.E.; Sandalova, T.; Tittmann, K.; Fiedler, E.; Neef, H.; Konig, S.; Kluger, R.; Kochetov, G.A.; Schneider, G.; Hubner, G.
Effect of coenzyme modification on the structural and catalytic properties of wild-type transketolase and of the variant E418A from Saccharomyces cerevisiae
Febs J.
272
1326-1342
2005
Saccharomyces cerevisiae
Selivanov, V.A.; Kovina, M.V.; Kochevova, N.V.; Meshalkina, L.E.; Kochetov, G.A.
Kinetic study of the H103A mutant yeast transketolase
FEBS Lett.
567
270-274
2004
Saccharomyces cerevisiae
Selivanov, V.A.; Kovina, M.V.; Kochevova, N.V.; Meshalkina, L.E.; Kochetov, G.A.
Studies of thiamin diphosphate binding to the yeast apotransketolase
J. Mol. Catal. B
26
33-40
2003
Saccharomyces cerevisiae
-
Esakova, O.A.; Khanova, E.A.; Meshalkina, L.E.; Golbik, R.; Huebner, G.; Kochetov, G.A.
Effect of transketolase substrates on holoenzyme reconstitution and stability
Biochemistry
70
770-776
2005
Saccharomyces cerevisiae
Sevostyanova, I.A.; Solovjeva, O.N.; Kochetov, G.A.
Two methods for determination of transketolase activity
Biochemistry
71
560-562
2006
Saccharomyces cerevisiae
Ospanov, R.V.; Kochetov, G.A.; Kurganov, B.I.
Influence of donor substrate on kinetic parameters of thiamine diphosphate binding to transketolase
Biochemistry
72
84-92
2007
Saccharomyces cerevisiae
Ospanov, R.; Kochetov, G.; Kurganov, B.
Theoretical model of interactions between ligand-binding sites in a dimeric protein and its application for the analysis of thiamine diphosphate binding to yeast transketolase
Biophys. Chem.
124
106-114
2006
Saccharomyces cerevisiae
Kochetov, G.A.; Sevostyanova, I.A.
Binding of the coenzyme and formation of the transketolase active center
IUBMB Life
57
491-497
2005
Saccharomyces cerevisiae
Esakova, O.A.; Meshalkina, L.E.; Kochetov, G.A.
Effects of transketolase cofactors on its conformation and stability
Life Sci.
78
8-13
2005
Saccharomyces cerevisiae
Sevestre, A.; Charmantray, F.; Helaine, V.; Lasikova, A.; Hecquet, L.
Synthesis of stereochemical probes for new fluorogenic assays for yeast transketolase variants
Tetrahedron
62
3969-3976
2006
Saccharomyces cerevisiae
-
Yurshev, V.A.; Sevostyanova, I.A.; Solovjeva, O.N.; Zabrodskaya, S.V.; Kochetov, G.A.
Nonequivalence of transketolase active centers with respect to acceptor substrate binding
Biochem. Biophys. Res. Commun.
361
1044-1047
2007
Saccharomyces cerevisiae
Meshalkina, L.E.; Kochetov, G.A.; Brauer, J.; Huebner, G.; Tittmann, K.; Golbik, R.
New evidence for cofactors amino group function in thiamin catalysis by transketolase
Biochem. Biophys. Res. Commun.
366
692-697
2008
Saccharomyces cerevisiae
Ospanov, R.V.; Kochetov, G.A.; Kurganov, B.I.
Influence of donor substrate on kinetic parameters of thiamine diphosphate binding to transketolase
Biochemistry (Moscow)
72
84-92
2007
Saccharomyces cerevisiae
Sevostyanova, I.A.; Yurshev, V.A.; Solovjeva, O.N.; Zabrodskaya, S.V.; Kochetov, G.A.
Effect of bivalent cations on the interaction of transketolase with its donor substrate
Proteins
71
541-545
2008
Saccharomyces cerevisiae
Charmantray, F.; Helaine, V.; Lasikova, A.; Legeret, B.; Hecquet, L.
Chemoenzymatic synthesis of L-tyrosine derivative for a transketolase assay
Tetrahedron Lett.
49
3229-3233
2008
Saccharomyces cerevisiae
-
Sevostyanova, I.A.; Selivanov, V.A.; Yurshev, V.A.; Solovjeva, O.N.; Zabrodskaya, S.V.; Kochetov, G.A.
Cooperative binding of substrates to transketolase from Saccharomyces cerevisiae
Biochemistry (Moscow)
74
789-792
2009
Saccharomyces cerevisiae
Matsushika, A.; Goshima, T.; Fujii, T.; Inoue, H.; Sawayama, S.; Yano, S.
Characterization of non-oxidative transaldolase and transketolase enzymes in the pentose phosphate pathway with regard to xylose utilization by recombinant Saccharomyces cerevisiae
Enzyme Microb. Technol.
51
16-25
2012
Saccharomyces cerevisiae (P23254), Saccharomyces cerevisiae (P33315), Saccharomyces cerevisiae
Solovjeva, O.N.; Sevostyanova, I.A.; Yurshev, V.A.; Selivanov, V.A.; Kochetov, G.A.
Effects of free Ca2+ on kinetic characteristics of holotransketolase
Protein J.
31
137-140
2012
Saccharomyces cerevisiae
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
-
Kochetov, G.A.; Solovjeva, O.N.
Structure and functioning mechanism of transketolase
Biochim. Biophys. Acta
1844
1608-1618
2014
Saccharomyces cerevisiae (P23254), Saccharomyces cerevisiae
Solovjeva, O.N.; Kovina, M.V.; Kochetov, G.A.
Substrate inhibition of transketolase
Biochim. Biophys. Acta
1864
280-282
2016
Saccharomyces cerevisiae (P23254)
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