Information on EC 2.2.1.1 - transketolase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.2.1.1
-
RECOMMENDED NAME
GeneOntology No.
transketolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
keto group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Bifidobacterium shunt
-
-
Biosynthesis of ansamycins
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Calvin-Benson-Bassham cycle
-
-
Carbon fixation in photosynthetic organisms
-
-
formaldehyde assimilation II (RuMP Cycle)
-
-
formaldehyde assimilation III (dihydroxyacetone cycle)
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Pentose phosphate pathway
-
-
pentose phosphate pathway (non-oxidative branch)
-
-
pentose phosphate pathway (partial)
-
-
Rubisco shunt
-
-
superpathway of glucose and xylose degradation
-
-
pentose phosphate pathway
-
-
photosynthesis
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoforms Tkt7 and Tkt10; isoform Tkt3
-
-
Manually annotated by BRENDA team
cultivar Jinyou 3
UniProt
Manually annotated by BRENDA team
K12
-
-
Manually annotated by BRENDA team
strain SN-G42 and 124A
-
-
Manually annotated by BRENDA team
strain SN-G42 and 124A
-
-
Manually annotated by BRENDA team
Balb-c mice
UniProt
Manually annotated by BRENDA team
clone NF54
-
-
Manually annotated by BRENDA team
overexpression in Escherichia coli
-
-
Manually annotated by BRENDA team
sugarcane
-
-
Manually annotated by BRENDA team
wheat, cv. Sappo
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
enzyme knockdown suppresses HCC cell proliferation by inducing reactive eoxygen species accumulation and reactive oxygen species-associated cell-cycle delay
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 D-xylulose 5-phosphate
glyceraldehyde 3-phosphate + glycolaldehyde
show the reaction diagram
-
reversible single substrate reaction, about 6% of the double-substrate reaction rate
-
-
?
2-deoxy-D-erythrose 4-phosphate + ?
?
show the reaction diagram
-
-
-
-
?
2-deoxy-D-ribose 5-phosphate + ?
?
show the reaction diagram
-
-
-
-
?
beta-hydroxypyruvate + ?
?
show the reaction diagram
-
-
-
-
?
beta-hydroxypyruvate + glycolaldehyde
L-erythrulose + CO2
show the reaction diagram
butanal + glycolaldehyde
(3S)-1,3-dihydroxyhexan-2-one
show the reaction diagram
-
-
-
-
?
butanal + hydroxypyruvate
1,3-dihydroxyhexan-2-one + CO2
show the reaction diagram
-
-
-
?
butyraldehyde + hydroxypyruvate
? + CO2
show the reaction diagram
-
-
-
?
D-arabinose 5-phosphate + ?
?
show the reaction diagram
-
-
-
-
?
D-erythrose + ?
?
show the reaction diagram
-
-
-
-
?
D-erythrose 4-phosphate + ?
?
show the reaction diagram
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
show the reaction diagram
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
erythrose 4-phosphate + D-xylulose 5-phosphate
show the reaction diagram
D-fructose 6-phosphate + D-ribose 5-phosphate
?
show the reaction diagram
D-fructose 6-phosphate + D-ribose 5-phosphate
D-erythrose 4-phosphate + sedoheptulose 7-phosphate
show the reaction diagram
-
-
-
?
D-fructose 6-phosphate + Fe(CN)3-
glycolic acid + D-erythrose 4-phosphate + Fe(CN)64- + H+
show the reaction diagram
D-glucose 6-phosphate + hydroxypyruvate
2-D-glycero-D-ido-octulose phosphate + ?
show the reaction diagram
-
reaction is catalyzed by either isoform Tkt7 or isoform Tkt10 or both
-
-
-
D-glyceraldehyde + hydroxypyruvate
D-ribulose + ?
show the reaction diagram
-
-
-
?
D-glyceraldehyde + hydroxypyruvate
D-xylulose + CO2
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-lactaldehyde + hydroxypyruvate
5-deoxy-D-ribulose + ?
show the reaction diagram
-
-
-
?
D-ribose + ?
?
show the reaction diagram
-
-
-
-
?
D-ribose + hydroxypyruvate
? + CO2
show the reaction diagram
-
-
-
?
D-ribose 5-phosphate + 2,3-dihydroxy-4-O-(2'-oxo-benzopyran-7'-yl)-D-threose
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
show the reaction diagram
D-threose 4-phosphate + ?
?
show the reaction diagram
-
-
-
-
?
D-xylose + ?
?
show the reaction diagram
-
-
-
-
?
D-xylulose 5-phosphate + D-erythrose 4-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
D-xylulose 5-phosphate + D-ribose 5-phosphate
?
show the reaction diagram
-
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
D-xylulose-5-phosphate + D-ribose-5-phosphate
?
show the reaction diagram
-
-
-
?
DL-glyceraldehyde + ?
?
show the reaction diagram
-
-
-
-
?
DL-glyceraldehyde + hydroxypyruvate
? + CO2
show the reaction diagram
-
-
-
?
DL-glyceraldehyde 3-phosphate + ?
?
show the reaction diagram
formaldehyde + ?
?
show the reaction diagram
-
-
-
-
?
fructose 6-phosphate + ?
?
show the reaction diagram
fructose-6-phosphate + hydroxypyruvate
?
show the reaction diagram
-
-
-
-
?
glyceraldehyde 3-phosphate + D-glyceraldehyde 3-phosphate
D-xylulose 5-phosphate + D-xylulose 5-phosphate
show the reaction diagram
-
-
-
-
r
glycolaldehyde + ?
?
show the reaction diagram
-
-
-
-
?
glycolaldehyde + hydroxypyruvate
L-erythrulose + CO2
show the reaction diagram
-
-
-
?
hydroxypyruvate + ?
?
show the reaction diagram
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
show the reaction diagram
hydroxypyruvate + ferricyanide + H2O
glycolic acid + ferrocyanide + ?
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + glycolaldehyde
erythrulose + ?
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + glycolaldehyde
L-erythrulose + ?
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + ribose 5-phosphate
sedoheptulose 7-phosphate + ?
show the reaction diagram
L-arabinose + ?
?
show the reaction diagram
-
-
-
-
?
L-erythrulose + D-ribose-5-phosphate
D-sedoheptulose 7-phosphate + glycolaldehyde
show the reaction diagram
-
-
-
?
L-erythrulose + ribose 5-phosphate
?
show the reaction diagram
L-glyceraldehyde + hydroxypyruvate
L-ribulose + ?
show the reaction diagram
minor reactivity
-
-
?
L-lactaldehyde + hydroxypyruvate
5-deoxy-L-ribulose + ?
show the reaction diagram
minor reactivity
-
-
?
L-lyxose + ?
?
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
-
-
-
-
?
methoxyethanal + glycolaldehyde
(3S)-1,3-dihydroxy-4-methoxybutan-2-one
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
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
-
-
?
propanal + glycolaldehyde
(3S)-1,3-dihydroxypentan-2-one
show the reaction diagram
-
-
-
-
?
propanal + lithium beta-hydroxypyruvate
(3S)-1,3-dihydroxypentan-2-one + (3R)-1,3-dihydroxypentan-2-one
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
ribulose 5-phosphate + ribose 5-phosphate
a heptulose phosphate + glyceraldehyde 3-phosphate
show the reaction diagram
-
ribulose is cleaved and ribose acts as acceptor
-
-
?
sedoheptulose 7-phosphate + ?
?
show the reaction diagram
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
show the reaction diagram
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
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
?
show the reaction diagram
-
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
D-xylulose-5-phosphate + D-ribose-5-phosphate
?
show the reaction diagram
A0A0I9QGZ2
-
-
-
?
glyceraldehyde 3-phosphate + D-glyceraldehyde 3-phosphate
D-xylulose 5-phosphate + D-xylulose 5-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
show the reaction diagram
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 hide
LITERATURE
IMAGE
thiamine diphosphate
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
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
activates
Cu2+
-
activates
Mn2+
-
activates
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(3-chloro-2-methylphenyl)-3-(2-hydroxy-5-nitrophenyl)urea
-
inhibitor designed to cover a hot spot in the dimerization interface of the homodimer of the enzyme
1-(5-chloro-2-hydroxy-4-nitrophenyl)-3-phenylurea
-
inhibitor designed to cover a hot spot in the dimerization interface of the homodimer of the enzyme
1-(5-hydroxynaphthalen-1-yl)-3-(2-methyl-5-nitrophenyl)urea
-
inhibitor designed to cover a hot spot in the dimerization interface of the homodimer of the enzyme
3-(6-methyl-2-amino-pyridin-3-ylmethyl)-5-(2-hydroxy-ethyl)-4-methyl-thiazol-3-ium chloride hydrochloride
4'-methylamino-thiamine diphosphate
-
cofactor analogue
D-arabinose 5-phosphate
D-ribose 5-phosphate
-
exerts a time-dependent inhibiting action on enzyme activity in the presence of NaCNBH3
D-ribose-5-phosphate
substrate inhibition above 50 mM
deazathiamine
-
retains thiamine pyrophosphokinase activity. Despite improvements in binding to transketolase in enzymatic assays, cell potency relative to the thiazolones and charged thiamine mimetics decrease
fructose 6-phosphate
at concentrations higher than 10 mM fructose 6-phosphate causes an inhibition of the enzyme
glycolaldehyde
-
-
Hg2+
-
-
L-erythrulose
-
competitive inhibition
N-Acetylimidazole
-
inhibition kinetics
N1'-methyl-thiamine diphosphate
-
cofactor analogue
N3'-pyridyl-thiamine
-
inactive analogue of thiamine diphosphate
N3P-TT
-
an aminopyridine, which possesses low micromolar cellular potency against transketolase
Oxythiamine
Oxythiamine diphosphate
p-hydroxyphenylpyruvate
-
potent inhibitor when hydroxypyruvate is used as a substrate, whereas noncompetitive inhibition with fructose-6-phosphate
PCMB
-
reversible by cysteine
Phenylglyoxal
-
prevents reconstitution of apotransketolase
phosphate
Phosphate buffer
-
20 mM phosphate buffer shows an inhibitory effect of the enzyme activity of approximately 40%
-
Rabbit antibodies
-
RNAi
-
sulfate
thiamine thiazolone
-
retains thiamine pyrophosphokinase activity, is a significantly better binder to transketolase than thiamine
thiamine thiazolone diphosphate
-
is a significantly better binder to transketolase than thiamine
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
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benfotiamine
-
; not inhibitory on proliferation of insulinoma cell line INS-1. Treatment activates glucose metabolism in INS-1 cells in high-glucose culture conditions and maximizes the cells' ability to synthesize insulin. Treatment activates glucokinase
cysteine
-
activation, 10 mM
ethanol
-
activation, 1-10% v/v
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
Oxythiamine
inhibitor of human enzyme, is not inhibitory up to 0.03 mM. Instead, oxythiamine, at this concentration, increases the rate of the reaction by 30% under the assay conditions tested
thiamin
-
increases abnormal erythrocyte transketolase activity
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
D,L-glyceraldehyde
-
-
2.1
D,L-glyceraldehyde 3-phosphate
-
-
150
D-erythrose
-
-
0.09 - 0.36
D-erythrose 4-phosphate
0.25 - 0.72
D-fructose 6-phosphate
6
D-glyceraldehyde
-
at pH 7.2 and 50°C
0.67 - 0.92
D-glyceraldehyde 3-phosphate
8.4
D-Lactaldehyde
-
at pH 7.2 and 50°C
230
D-ribose
-
-
0.007 - 7
D-ribose 5-phosphate
0.13 - 2.75
D-ribose-5-phosphate
45
D-xylose
-
-
0.0056 - 4.08
D-xylulose 5-phosphate
31
formaldehyde
-
-
0.61 - 11
fructose 6-phosphate
2.25
fructose-6-phosphate
-
-
4.9
glyceraldehyde 3-phosphate
-
-
14 - 200
glycolaldehyde
4.78 - 33
Hydroxypyruvate
55
L-arabinose
-
-
4.9 - 8
L-erythrulose
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
120
L-Lyxose
-
-
26
lithium beta-hydroxypyruvate
-
pH 7.0, 25°C
55 - 140
propionaldehyde
4
sedoheptulose 7-phosphate
-
-
0.0003 - 0.007
thiamine diphosphate
0.0365 - 0.16
Xylulose 5-phosphate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3 - 4.9
2-deoxy-D-erythrose 4-phosphate
0.3 - 0.4
2-deoxy-D-ribose 5-phosphate
0.05 - 0.4
D-arabinose 5-phosphate
1.4 - 69
D-erythrose 4-phosphate
82 - 112
D-fructose 6-phosphate
48 - 99
D-glyceraldehyde 3-phosphate
0.0148 - 56.7
D-ribose 5-phosphate
8.4
D-ribose-5-phosphate
Leishmania mexicana
Q8MPM3
pH 7.5
0.07 - 0.3
D-threose 4-phosphate
0.05 - 54
D-xylulose 5-phosphate
0.002 - 44.5
Hydroxypyruvate
410000
lithium beta-hydroxypyruvate
Escherichia coli
-
pH 7.0, 25°C
0.0187 - 56.7
Xylulose 5-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
115 - 448
D-fructose 6-phosphate
87
71 - 108
D-glyceraldehyde 3-phosphate
147
84 - 109
D-ribose 5-phosphate
183
231 - 264
D-xylulose 5-phosphate
644
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.305
p-hydroxyphenylpyruvate
-
with hydroxypyruvate as substrate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
1-(3-chloro-2-methylphenyl)-3-(2-hydroxy-5-nitrophenyl)urea
Homo sapiens
-
pH 7.6, 37°C
0.1
1-(5-chloro-2-hydroxy-4-nitrophenyl)-3-phenylurea
Homo sapiens
-
pH 7.6, 37°C
0.15
1-(5-hydroxynaphthalen-1-yl)-3-(2-methyl-5-nitrophenyl)urea
Homo sapiens
-
pH 7.6, 37°C
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
0.14
-
mutant D469T, mutant R520V and mutant R520Stop, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0; mutant R520Stop, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.16
-
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
0.42
-
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
0.77
-
crude extract with 4 mg/l added thiamine
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
1.95
-
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
2.3
-
mutant R520Stop, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0; mutant R520V, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
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
3.2 - 3.9
-
-
3.64
-
pH 7.6, 22°C
5.5
-
recombinant enzyme, pH 7.6, 30°C
9.5
-
mutant C160E, pH 7.6, 25°C
10.27
-
-
21.8
-
mutant C160S, pH 7.9, 25°C
30.1
-
mutant C160D, pH 8.5, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 7.8
-
R359A, R528A
6.6 - 7.4
-
H481Q
6.6 - 7.8
-
H469A
6.8 - 7.8
-
D477A
7 - 7.5
-
in phosphate buffer
7.5 - 8.6
-
-
7.5 - 7.6
7.5 - 7.8
-
H69A
7.5 - 7.6
-
-
7.5 - 8.5
7.6 - 7.8
-
-
7.6 - 8
-
-
7.6 - 8.2
-
wild-type
7.8
-
mutant C160A; wild-type
7.8 - 8.2
-
-
7.9
-
mutant C160S
8 - 8.5
8.5
-
mutant C160D
8.5 - 9
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 11
-
more than 50% of maximum activity
5.5 - 8.5
more than 50% activity between pH 5.5 and 8.5
5.8 - 9.5
-
about half-maximal activity at pH 5.8 and 9.5
6 - 8
-
more than 80% of maximum activity
6.5 - 10.2
-
about half-maximal activity at pH 6.5 and 10.2
6.5 - 10.5
-
about half-maximal activity at pH 6.5 and about 60% of maximal activity at pH 10.5
6.8 - 9
-
about half-maximal activity at pH 6.8 and 9.0
7.1 - 9.5
-
about half-maximal activity at pH 7.1 and 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
45
-
assay at, low enzyme concentration
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 70
more than 50% activity from 40 to 70°C with a sharp decrease thereafter leaving about 25% and 0% activity at 75°C and 85°C, respectively
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
ganglion cells in medulla
Manually annotated by BRENDA team
-
at the lesion border
Manually annotated by BRENDA team
-
adult bone marrow-derived insulin-producing cells, presence of transketolase protein under high-glucose conditions
Manually annotated by BRENDA team
-
only 29% of non-neoplastic breast tissues are TKTL1 immunopositive, including 9% with high expression levels
Manually annotated by BRENDA team
-
TKTL1 expression in 86% of breast cancer specimens with 45% showing high expression levels
Manually annotated by BRENDA team
-
thiamine-deficinet diet reduces transketolase activity in both cortex and hippocampus, without significantly affecting the activities of pyruvate dehydrogenase, alpha-ketoglutamate dehydrogenase, and glucose 6-phosphate dehydrogenase
Manually annotated by BRENDA team
-
normal and multiple sclerosis samples
Manually annotated by BRENDA team
-
compared with grades II and III astrocytic gliomas, glioblastoma multiformes show higher expression of TKTL1