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Information on EC 2.2.1.1 - transketolase and Organism(s) Homo sapiens and UniProt Accession P29401

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     2 Transferases
         2.2 Transferring aldehyde or ketonic groups
             2.2.1 Transketolases and transaldolases
                2.2.1.1 transketolase
IUBMB Comments
A thiamine-diphosphate protein. Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO2 and R-CHOH-CO-CH2OH. The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.
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Homo sapiens
UNIPROT: P29401
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
transketolase, tktl1, transketolase a, transketolase-like 1, tktl-1, transketolase-like-1, tktl2, transketolase-like enzyme 1, transketolase-like-2, tkt10, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycolaldehydetransferase
-
-
-
-
TKTL-1
-
-
TKTL1
transketolase like 1
-
-
transketolase-like 1
transketolase-like enzyme 1
transketolase-like-1
transketolase-like-1-gene
-
-
transketolase-like-2
-
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
formation of the central 1,2-dihydroxyethyl-thiamine diphosphate carbanion-enamine intermediate is thermodynamically favored with increasing carbon chain length of the donor ketose substrate
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
keto group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glycolaldehydetransferase
A thiamine-diphosphate protein. Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO2 and R-CHOH-CO-CH2OH. The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-48-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-erythrose 4-phosphate + D-xylulose 5-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
show the reaction diagram
-
-
-
r
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
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
-
-
?
D-erythrose 4-phosphate + ?
?
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + D-ribose 5-phosphate
?
show the reaction diagram
-
40% as effective as D-xylulose 5-phosphate
-
-
?
D-fructose 6-phosphate + Fe(CN)3-
glycolic acid + D-erythrose 4-phosphate + Fe(CN)64- + H+
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
r
D-xylulose 5-phosphate + D-erythrose 4-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
best acceptor with D-xylulose 5-phosphate as donor
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
fructose 6-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 SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-erythrose 4-phosphate + D-xylulose 5-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
show the reaction diagram
-
-
-
r
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-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
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
thiamine diphosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
presence of magnesium ions, alone or in combination with thiamine diphosphate, does not affect the activity
INHIBITOR
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
-
analog of thiamine, almost completely suppresses transketolase activity in blood, spleen, and tumor cells, but has little effect on activity of the other thiamine-utilizing enzymes alpha-ketoglutarate dehydrogenase or glucose-6-phosphate dehydrogenase
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
Hg2+
-
-
N3P-TT
-
an aminopyridine, which possesses low micromolar cellular potency against transketolase
oxythiamine
PCMB
-
reversible by cysteine
phosphate
-
not
Rabbit antibodies
-
anti-transketolase IgG, 20% inhibition
-
RNAi
-
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
additional information
-
activity of transketolase is significantly reduced in brains of alcoholic patients with Wernicke-Korsakoff’s Syndrome. Reduced transketolase protein expression levels in autopsied prefrontal white and grey matter and cerebellar vermis samples from neurologically uncomplicated alcoholics and alcoholics with liver cirrhosis
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
-
activation, 10 mM
ethanol
-
activation, 1-10% v/v
thiamin
-
increases abnormal erythrocyte transketolase activity
additional information
-
increased levels of TKTL1 transcript in tumors compared with their corresponding normal tissues. Positive correlation between TKTL1 protein expression in primary tumors and the number of metastatic lymph-nodes as well as the diameter of the largest metastatic area in lymph-nodes. High levels of TKTL1 transcript are a relevant phenomenon in small PTCs
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.48 - 0.61
D-ribose 5-phosphate
0.255 - 0.303
D-xylulose 5-phosphate
0.36
D-erythrose 4-phosphate
-
-
0.34
D-fructose 6-phosphate
-
pH 7.6, temperature not specified in the publication
0.063 - 0.63
D-ribose 5-phosphate
0.011 - 0.49
D-xylulose 5-phosphate
7
fructose 6-phosphate
-
-
0.0004
thiamine diphosphate
-
in the presence of Mg2+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.1 - 6.3
D-xylulose 5-phosphate
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
2.7
His-tagged recombinant enzyme, pH 7.6, 30°C
5.5
recombinant enzyme, pH 7.6, 30°C
10.27
-
-
3.2 - 3.9
-
-
3.64
-
pH 7.6, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.6
-
-
7.6 - 7.8
-
-
7.6 - 8
-
-
8 - 8.5
-
-
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
at the lesion border
Manually annotated by BRENDA team
in normal human brain transketolase is expressed on almost the totality of mature oligodendrocytes and scattered NG2-positive precursors, diffusely on ependymal cells and on distinct subsets of neuronal populations
Manually annotated by BRENDA team
normal and multiple sclerosis samples
Manually annotated by BRENDA team
at the lesion border
Manually annotated by BRENDA team
at the lesion border
Manually annotated by BRENDA team
transketolase is mainly expressed by oligodendrocytes in normal conditions, but is also present in oligodendrocytes in normal appearing white matter around multiple sclerosis plaques
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
compared with grades II and III astrocytic gliomas, glioblastoma multiformes show higher expression of TKTL1
Manually annotated by BRENDA team
transketolase activity is significantly higher in nasopharyngeal carcinoma tissues than in chronic nasopharyngitis tissues. TKTL1 in human nasopharyngeal carcinoma tissues is upregulated, whereas TKT is not upregulated
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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
-
the enzyme is fundamental in the non-oxidative branch of the pentose phosphate pathway
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TKT_HUMAN
623
0
67878
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
104000
-
gel filtration
135000
-
gel filtration
136000
-
-
60000
smaller splice variant, Western blot analysis
66000
-
alpha2, 2 * 66000, SDS-PAGE
67900
-
x * 68000, SDS-PAGE, x * 67900, calculated
68000
-
x * 68000, SDS-PAGE, x * 67900, calculated
70000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
alpha2, 2 * 66000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of inhibitors 1-(3-chloro-2-methylphenyl)-3-(2-hydroxy-5-nitrophenyl)urea, 1-(5-hydroxynaphthalen-1-yl)-3-(2-methyl-5-nitrophenyl)urea, 1-(5-chloro-2-hydroxy-4-nitrophenyl)-3-phenylurea into enzyme structure model. the binding mode of the compounds involves interactions with the alpha helix sequence D200-G210 interfering likely with the enzyme dimerization
to 1.75 A resolution, space group C2 with one monomer in the asymmetric unit. Two monomers form the homodimeric biological assembly with two identical active sites at the dimer interface. The protomer exhibits the typical three alpha/beta-domain structure and topology reported for transketolases from other species, with structural differences for several loop regions and the linker that connects the diphosphate and pyridine domain. Two lysines and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate and replaces an isoleucine found in most non-mammalian transketolases. The side chain of Gln428 forms a hydrogen bond with the 4-amino group of thiamine diphosphate and replaces a histidine that is invariant in all nonmammalian transketolases. All other amino acids involved in substrate binding and catalysis are strictly conserved. Formation of the central 1,2-dihydroxyethyl-thiamine diphosphate carbanion-enamine intermediate is thermodynamically favored with increasing carbon chain length of the donor ketose substrate
homology modeling of human transketolase using the crystal structure of yeast as a template, refinement of the model through molecular dynamics simulations. Five critical sites containing arginines R101, R318, R395, R401 and R474 contribute to dimer stability or catalytic activity. R101 and R401 maintain hydrogen bonds within the dimer, the most important being with D424 and E432, respectively. Both bonds are formed by charged residues. Non-conserved R395 also forms stable intermolecular hydrogen bonds. There is a substrate channel similar to the yeast enzyme
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
in vitro induction of the expression by arabinose decreases the amount of recombinant enzyme isolated and lowers its specific activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
albumin enhances thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dilution, stable to
-
freezing and thawing causes loss of activity
-
freezing and thawing, stable to
-
purification and storage lead to modification
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, 50 mM glycylglycine buffer, pH 7.6, no activity loss throughout several months
-
-20°C, 2 months
-
-20°C, stable
-
-90°C, several weeks
-
4°C, 50 mM glycylglycine buffer, pH 7.6, stable for several days
-
4°C, at least 16 days
-
4°C, several weeks
-
room temperature, after 13 days at 4°C, at least 4 h stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
-
recombinant protein
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in HEK-293T cells and Dictyostelium discoideum
-
expression in Escherichia coli
-
TKTL1 cloned into vector pEGFP-C1-U6
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme overexpression in cancer cells is a response of Nuclear Factor, Erythroid 2-Like 2 activation
-
in HeLa cells, transketolase-like enzyme 1 mRNA is specifically overexpressed compared with normal human endocervical epithelial cells
the enzyme is upregulated in metastatic peritoneal implants
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
transketolase may emerge as a target of multiple sclerosis cerebro-spinal fluid autoimmune response
drug development
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mocali, A.; Paoletti, F.
Transketolase from human leukocytes. Isolation, properties and induction of polyclonal antibodies
Eur. J. Biochem.
180
213-219
1989
Homo sapiens
Manually annotated by BRENDA team
Warnock, L.G.; Prudhomme, C.R.
The isolation and preliminary characterization of apotransketolase from human erythrocytes
Biochem. Biophys. Res. Commun.
106
719-723
1982
Homo sapiens
Manually annotated by BRENDA team
Takeuchi, T.; Nishino, K.; Itokawa, Y.
Purification and characterization of, and preparation of an antibody to, transketolase from human red blood cells
Biochim. Biophys. Acta
872
24-32
1986
Homo sapiens
Manually annotated by BRENDA team
Schellenberg, G.D.; Wilson, N.M.; Copeland, B.R.; Furlong, C.E.
Transketolase from human red blood cells
Methods Enzymol.
90
223-228
1982
Homo sapiens
Manually annotated by BRENDA team
Heinrich, P.C.; Wiss, O.
Transketolase from human erythrocytes. Purification and properties
Helv. Chim. Acta
54
2658-2668
1971
Homo sapiens
Manually annotated by BRENDA team
Schenk, G.; Duggleby, R.G.; Nixon, P.F.
Properties and functions of the thiamin diphosphate dependent enzyme transketolase
Int. J. Biochem. Cell Biol.
30
1297-1318
1998
Cyberlindnera jadinii, Oryctolagus cuniculus, Escherichia coli, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces pastorianus, Spinacia oleracea, Sus scrofa, Saccharomyces cerevisiae (P23254), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Voelker, H.U.; Hagemann, C.; Coy, J.; Wittig, R.; Sommer, S.; Stojic, J.; Haubitz, I.; Vince, G.H.; Kaemmerer, U.; Monoranu, C.M.
Expression of transketolase-like 1 and activation of Akt in grade IV glioblastomas compared with grades II and III astrocytic gliomas
Am. J. Clin. Pathol.
130
50-57
2008
Homo sapiens (P51854)
Manually annotated by BRENDA team
Hu, L.H.; Yang, J.H.; Zhang, D.T.; Zhang, S.; Wang, L.; Cai, P.C.; Zheng, J.F.; Huang, J.S.
The TKTL1 gene influences total transketolase activity and cell proliferation in human colon cancer LoVo cells
Anticancer Drugs
18
427-433
2007
Homo sapiens
Manually annotated by BRENDA team
Thomas, A.A.; Le Huerou, Y.; De Meese, J.; Gunawardana, I.; Kaplan, T.; Romoff, T.T.; Gonzales, S.S.; Condroski, K.; Boyd, S.A.; Ballard, J.; Bernat, B.; DeWolf, W.; Han, M.; Lee, P.; Lemieux, C.; Pedersen, R.; Pheneger, J.; Poch, G.; Smith, D.; Sullivan, F.; Weiler, S.; Wright, S.K.; Lin, J.; Brandhuber, B.; Vigers, G.
Synthesis, in vitro and in vivo activity of thiamine antagonist transketolase inhibitors
Bioorg. Med. Chem. Lett.
18
2206-2210
2008
Homo sapiens
Manually annotated by BRENDA team
Thomas, A.A.; De Meese, J.; Le Huerou, Y.; Boyd, S.A.; Romoff, T.T.; Gonzales, S.S.; Gunawardana, I.; Kaplan, T.; Sullivan, F.; Condroski, K.; Lyssikatos, J.P.; Aicher, T.D.; Ballard, J.; Bernat, B.; DeWolf, W.; Han, M.; Lemieux, C.; Smith, D.; Weiler, S.; Wright, S.K.; Vigers, G.; Brandhuber, B.
Non-charged thiamine analogs as inhibitors of enzyme transketolase
Bioorg. Med. Chem. Lett.
18
509-512
2008
Homo sapiens
Manually annotated by BRENDA team
Zerilli, M.; Amato, M.C.; Martorana, A.; Cabibi, D.; Coy, J.F.; Cappello, F.; Pompei, G.; Russo, A.; Giordano, C.; Rodolico, V.
Increased expression of transketolase-like-1 in papillary thyroid carcinomas smaller than 1.5 cm in diameter is associated with lymph-node metastases
Cancer
113
936-944
2008
Homo sapiens
Manually annotated by BRENDA team
Zhang, S.; Yue, J.X.; Yang, J.H.; Cai, P.C.; Kong, W.J.
Overexpression of transketolase protein TKTL1 is associated with occurrence and progression in nasopharyngeal carcinoma: a potential therapeutic target in nasopharyngeal carcinoma
Cancer Biol. Ther.
7
517-522
2008
Homo sapiens (P51854), Homo sapiens (Q9H0I9), Homo sapiens
Manually annotated by BRENDA team
Voelker, H.U.; Scheich, M.; Schmausser, B.; Kaemmerer, U.; Eck, M.
Overexpression of transketolase TKTL1 is associated with shorter survival in laryngeal squamous cell carcinomas
Eur. Arch. Otorhinolaryngol.
264
1431-1436
2007
Homo sapiens
Manually annotated by BRENDA team
Lonsdale, D.
Three case reports to illustrate clinical applications in the use of erythrocyte transketolase
Evid. Based. Complement Alternat. Med.
4
247-250
2006
Homo sapiens
Manually annotated by BRENDA team
Alexander-Kaufman, K.; Harper, C.
Transketolase: Observations in alcohol-related brain damage research
Int. J. Biochem. Cell Biol.
41
717-720
2009
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Krockenberger, M.; Honig, A.; Rieger, L.; Coy, J.F.; Sutterlin, M.; Kapp, M.; Horn, E.; Dietl, J.; Kammerer, U.
Transketolase-like 1 expression correlates with subtypes of ovarian cancer and the presence of distant metastases
Int. J. Gynecol. Cancer
17
101-106
2007
Homo sapiens
Manually annotated by BRENDA team
Froehlich, E.; Fink, I.; Wahl, R.
Is transketolase like 1 a target for the treatment of differentiated thyroid carcinoma? A study on thyroid cancer cell lines
Invest. New Drugs
27
297-303
2009
Homo sapiens
Manually annotated by BRENDA team
Kohrenhagen, N.; Voelker, H.U.; Schmidt, M.; Kapp, M.; Krockenberger, M.; Frambach, T.; Dietl, J.; Kammerer, U.
Expression of transketolase-like 1 (TKTL1) and p-Akt correlates with the progression of cervical neoplasia
J. Obstet. Gynaecol. Res.
34
293-300
2008
Homo sapiens (P51854)
Manually annotated by BRENDA team
Lovato, L.; Cianti, R.; Gini, B.; Marconi, S.; Bianchi, L.; Armini, A.; Anghileri, E.; Locatelli, F.; Paoletti, F.; Franciotta, D.; Bini, L.; Bonetti, B.
Transketolase and CNPase I are specifically recognized by IgG autoantibodies in multiple sclerosis patients
Mol. Cell. Proteomics
7
2337-2349
2008
Homo sapiens (P29401), Homo sapiens
Manually annotated by BRENDA team
Foeldi, M.; Stickeler, E.; Bau, L.; Kretz, O.; Watermann, D.; Gitsch, G.; Kayser, G.; Zur Hausen, A.; Coy, J.F.
Transketolase protein TKTL1 overexpression: A potential biomarker and therapeutic target in breast cancer
Oncol. Rep.
17
841-845
2007
Homo sapiens
Manually annotated by BRENDA team
Wu, H.T.; Allie, N.; Myer, L.; Govender, D.
Anaplastic nephroblastomas express transketolase-like enzyme 1
J. Clin. Pathol.
62
460-463
2009
Homo sapiens
Manually annotated by BRENDA team
Chen, H.; Yue, J.; Yang, S.; Ding, H.; Zhao, R.; Zhang, S.
Overexpression of transketolase-like gene 1 is associated with cell proliferation in uterine cervix cancer
J. Exp. Clin. Cancer Res.
28
43-55
2009
Homo sapiens (P51854), Homo sapiens
Manually annotated by BRENDA team
Obiol-Pardo, C.; Rubio-Martinez, J.
Homology modeling of human transketolase: description of critical sites useful for drug design and study of the cofactor binding mode
J. Mol. Graph. Model.
27
723-734
2009
Homo sapiens
Manually annotated by BRENDA team
Meshalkina, L.E.; Solovjeva, O.N.; Kochetov, G.A.
Interaction of transketolase from human tissues with substrates
Biochemistry (Moscow)
76
1061-1064
2011
Homo sapiens
Manually annotated by BRENDA team
Meshalkina, L.E.; Solovjeva, O.N.; Khodak, Y.A.; Drutsa, V.L.; Kochetov, G.A.
Isolation and properties of human transketolase
Biochemistry (Moscow)
75
873-880
2010
Homo sapiens
Manually annotated by BRENDA team
Mitschke, L.; Parthier, C.; Schroeder-Tittmann, K.; Coy, J.; Luedtke, S.; Tittmann, K.
The crystal structure of human transketolase and new insights into its mode of action
J. Biol. Chem.
285
31559-31570
2010
Homo sapiens (P29401), Homo sapiens
Manually annotated by BRENDA team
Obiol-Pardo, C.; Alcarraz-Vizan, G.; Cascante, M.; Rubio-Martinez, J.
Diphenyl urea derivatives as inhibitors of transketolase: a structure-based virtual screening
PLoS ONE
7
e32276
2012
Homo sapiens (P29401), Homo sapiens
Manually annotated by BRENDA team
Sheng, X.; Liu, Y.; Liu, C.
Theoretical studies on the common catalytic mechanism of transketolase by using simplified models
J. Mol. Graph. Model.
39
23-28
2013
Homo sapiens (P29401)
Manually annotated by BRENDA team
Xu, I.M.; Lai, R.K.; Lin, S.H.; Tse, A.P.; Chiu, D.K.; Koh, H.Y.; Law, C.T.; Wong, C.M.; Cai, Z.; Wong, C.C.; Ng, I.O.
Transketolase counteracts oxidative stress to drive cancer development
Proc. Natl. Acad. Sci. USA
113
725-734
2016
Homo sapiens
Manually annotated by BRENDA team
Prejano, M.; Medina, F.E.; Fernandes, P.A.; Russo, N.; Ramos, M.J.; Marino, T.
The catalytic mechanism of human transketolase
Chemphyschem
20
2881-2886
2019
Homo sapiens (P29401), Homo sapiens
Manually annotated by BRENDA team
Ricciardelli, C.; Lokman, N.A.; Cheruvu, S.; Tan, I.A.; Ween, M.P.; Pyragius, C.E.; Ruszkiewicz, A.; Hoffmann, P.; Oehler, M.K.
Transketolase is upregulated in metastatic peritoneal implants and promotes ovarian cancer cell proliferation
Clin. Exp. Metastasis
32
441-455
2015
Homo sapiens
Manually annotated by BRENDA team
Mesquita, A.; Tabara, L.C.; Martinez-Costa, O.; Santos-Rodrigo, N.; Vincent, O.; Escalante, R.
Dissecting the function of Atg1 complex in Dictyostelium autophagy reveals a connection with the pentose phosphate pathway enzyme transketolase
Open Biology
5
150088
2015
Homo sapiens
Manually annotated by BRENDA team