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
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analysis
- 2.2.1.1
- thiamin
- pentose
- erythrocyte
- pyrophosphate
- transaldolase
- glucose-6-phosphate
- tpp
- ribose
- 5-phosphate
- aldolase
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non-oxidative
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glycation
- encephalopathy
- pyridoxine
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apoenzyme
- phosphoglycerate
- wernicke
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baker
- oxythiamine
- neuropathy
- ribose-5-phosphate
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thiamine-deficient
- xylulose
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thiamine-dependent
- 6-phosphogluconate
- riboflavin
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calvin
- pharmacology
- drug development
- biotechnology
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pentose-phosphate
- xylulokinase
- industry
- alpha-ketoglutarate
- dihydroxyacetone
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warburg
- phosphoketolase
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3-epimerase
- hemolysates
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pyrophosphokinase
- xylitol
- phosphoribulokinase
- thiaminase
- hydroxypyruvate
- aminopyrimidine
- fructose-6-phosphate
- medicine
- fructose-1,6-bisphosphate
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antivitaminous
- erythrose
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egypt
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thdp-dependent
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diphosphate-dependent
- synthesis
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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
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Application
Application on EC 2.2.1.1 - transketolase
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analysis
biotechnology
drug development
industry
medicine
pharmacology
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benfotiamine treatment activates glucose metabolism in INS-1 cells in high-glucose culture conditions and maximizes the cells' ability to synthesize insulin. Treatment activates glucokinase
synthesis
additional information
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low cost, rapid colorimetric transketolase assay, able to detect value above 8% bioconversion using non-alpha-hydroxylated aldehydes as acceptor substrates. The assay is significantly faster and more convenient to use than HPLC and can be used with a range of aliphatic and aromatic aldehydes. In addition, analysis of the alpha,alpha'-dihydroxyketone produced in the bioconversion can be quantified using this assay system with high-throughput. Furthermore, this method has the potential to be used to screen other chemical reactions or bioconversions leading to the formation of products possessing a 2-hydroxyketone motif
analysis
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a rapid microplate-based approach for measuring the denaturation curves by intrinsic tryptophan fluorescence for simple monomeric and two-state unfolding proteins like transketolase
analysis
coupling of a transketolase reaction that converts D-fructose 6-phosphate to D-erythrose 4-phosphate, which can then be converted to 4-phosphate D-erythronate using erythrose-4-phosphate dehydrogenase, a reaction that reduces NAD+ to NADH and can be easily followed spectrophotometrically
analysis
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establishment of a rapid microplate-based HPLC assay for transketolase, for rapidly determining substrate and product concentration suitable for optimisation of biocatalytic process conditions and screening directed evolution libraries, which can be used to determine transketolase activity with a throughput of up to 1200 samples per day, whereas the well-to-well variation from HPLC measurement is just 1.9% for the lowest activities measured
analysis
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highly effective, stable and sensitive method for measuring TKT activity, incorporating xylulokinase, which induces generation of xylulose 5-phosphate from xylulose, from Saccharomyces cerevisiae into conventional TKT assay
analysis
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tetrazolium red-based colorimetric assay to screen for transketolase activity with a range of aldehyde acceptors. The assay is able to detect >8% bioconversion using non-alpha-hydroxylated aldehydes as acceptor substrates and is significantly faster and more convenient to use than chromatographic procedures
analysis
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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
analysis
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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
improvement of biocatalytic processes using transketolase over prolonged reaction times will need to address the formation of cofactor-associated intermediate state
biotechnology
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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
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non-permanently charged thiamine mimetics (thiamine analogs possessing B-rings unable to participate in the cycle) are competent substrates for thiamine pyrophosphokinase, and the resulting pyrophosphates antagonize the activity of transketolase in vitro. Despite remarkable potencies in enzymatic assays, cellular potencies are modest to poor. Inhibition of the thiamine-utilizing enzyme transketolase is linked with diminished tumor cell proliferation
drug development
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Plasmodium falciparum transketolase shows low homology with the host enzyme, thus may serve as a novel and promising target for designing inhibitors with anti-malarial activity
drug development
ring-opened analogs of the transketolase inhibitor 'N30-pyridyl thiamine'; 3-(6-methyl-2-amino-pyridin-3-ylmethyl)-5-(2-hydroxy-ethyl)-4-methyl-thiazol-3-ium chloride hydrochloride are effectively transformed in vivo to the active thiazoliums, whereby the effectiveness of this transformation is dependent on the sulfur moiety. The pharmacokinetic properties of the transketolase inhibitor are improved, the Cmax is reduced, thus avoiding toxicity, and higher distribution and exposure correlate in vivo with a stronger and longer inhibition of blood transketolase
drug development
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ring-opened analogs of the transketolase inhibitor 'N30-pyridyl thiamine'; 3-(6-methyl-2-amino-pyridin-3-ylmethyl)-5-(2-hydroxy-ethyl)-4-methyl-thiazol-3-ium chloride hydrochloride are effectively transformed in vivo to the active thiazoliums, whereby the effectiveness of this transformation is dependent on the sulfur moiety. The pharmacokinetic properties of the transketolase inhibitor are improved, the Cmax is reduced, thus avoiding toxicity, and higher distribution and exposure correlate in vivo with a stronger and longer inhibition of blood transketolase
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production of abundant intermediates for industrially erythritol production
industry
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production of abundant intermediates for industrially erythritol production
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both TKTL1 and p-Akt play an important role in the progression of cervical neoplasia, which may be due to their impact on glycolysis. Intensity of the expression of TKTL1 and the oncogene p-Akt increases significantly with an increase in the histopathological grade of cervical tissues. TKTL1 and p-Akt can be possibly valuable targets for nontoxic antitumor therapeutic approaches, especially in cervical precancerous lesions and cancer
medicine
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initially abnormal erythrocyte transketolase activity and/or the thiamin pyrophosphate effect, indicating intracellular cofactor deficiency, usually improves with thiamin administration
medicine
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is crucial for optimal brain function. Abnormal transketolase expression and/or activity are implicated in a number of diseases where thiamin availability is low, including Wernicke-Korsakoffs Syndrome and alcoholism
medicine
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marked subset of breast cancers show a TKTL1 overexpression which correlates significantly with Her2/neu overexpression. In contrast to colon and urothelial cancer from previous studies, TKTL1 overexpression is not associated with a poor patient outcome in the examined study population. TKTL1 represents a novel metabolic biomarker in breast cancer, and a possible future target for mechanism-driven drug development
medicine
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the transketolase-like-1 gene plays an important role in total transketolase activity and in cell proliferation of human colon cancer. Transketolase-like-1 may serve as a target for novel anticancer therapies
medicine
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TktA interacts with MarR. TktA decreases MarR repressor activity. Overexpressing tktA decreases antibiotic susceptibility. Endogenous TktA enhances multiple antibiotic resistance to a small degree through release of MarR repression of the marRAB operon
medicine
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TKTL 1 is highest expressed in cell lines derived from more invasive tumors but the expression level is not strongly correlated to proliferation rate, to GLUT-1 expression or to the response to oxythiamine. Overexpression of TKTL-1 is not an indicator for responsiveness to oxythiamine
medicine
TKTL1 gene influences total transketolase activity and cell proliferation in human nasopharyngeal carcinoma cells, suggesting that TKTL1 gene plays an important role on glycometabolism in tumors and may become a novel target for tumor gene therapy
medicine
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TKTL1 overexpression in papillary thyroid carcinoma bigger than 1.5 cm may be considered a factor that facilitates tumor growth and progression. Significant association between TKTL1 protein expression and the presence of multifocality, bilaterality, extrathyroidal extension, vascular invasion, sclerosis, and lymph-node metastases
medicine
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TKTL1 overexpression is associated with a more aggressive behavior and shorter survival of laryngeal squamous cell carcinomas
medicine
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TKTL1 plays a crucial role in ovarian cancer metabolism and its expression predicts poor prognosis. TKTL1 could thus have a possible value as target for nontoxic antitumoral therapeutic approaches especially in advanced ovarian cancer, a disease where really efficient treatment options are limited
medicine
transketolase may emerge as a target of multiple sclerosis cerebro-spinal fluid autoimmune response
medicine
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treatment of hyperglycemic mice with BM-derived IPCs transplantation and benfotiamine, whereby activation of transketolase by benfotiamine can be playing a significant role in upregulation of both glucose metabolism and insulin protein synthesis
medicine
upregulation of TKTL1 in the metabolism of astrocytic gliomas with different degrees of malignancy. Percentage of positive cells for TKTL1 and p-Akt are significantly correlated. These observations can lead to additional therapeutic options targeting a specific blockade of TKTL1 enzyme activity
medicine
in HeLa cells, transketolase-like enzyme 1 mRNA is specifically overexpressed compared with normal human endocervical epithelial cells. After anti-transketolase-like enzyme 1 siRNA treatment, total transketolase activity is significantly reduced and cell proliferation is remarkably inhibited. In endocervical epithelia cells, total transketolase activity and cell proliferation have no significant differences after siRNA treatment
medicine
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six out of 15 anaplastic nephroblastomas analyzed show staining of transketolase-like enzyme 1 in 80100% of the tumour. None of the 13 non-anaplastic nephroblastomas analyzed shows transketolase-like enzyme 1 staining in more than 80% of the tumour. Transketolase-like enzyme 1 expression is associated with the presence of anaplasia and may be a mechanism via which anaplastic tumour cells thrive under different conditions
medicine
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high nuclear enzyme positivity in peritoneal metastases is significantly associated with reduced overall survival and a 2.8fold increased risk of ovarian cancer death
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desing of an enzyme microreaktor by reversible immobilization of His6-tagged enzyme a 200-microm ID fused silica capillary for quantitative kinetic analysis. Transketolase kinetic parameters in the mircoreactor are comparable with those measured in free solution. Quantitative elution of the immobilized transketolase and the regeneration and reuse of the derivatized capillary over five cycles are possible
synthesis
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mathematical model for the modes of operation in the reaction of beta-hydroxypyruvate and glycolaldehyde as an alternative to a batch process. The performance of the system strongly depends on the solubility of beta-hydroxypyruvate. The best option for the base case scenario is to use an initial beta-hydroxypyruvate concentration at its solubility level with a slight excess of glycolaldehyde and an initial catalyst concentration of 0.5 g/l for 120 min
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development of a comprehensive reaction model for a transketolase mediated carbon-carbon formation, based on the synthesis of erythrulose, which includes component degradation as a function of time and concentration as well as glycolaldehyde toxicity towards the enzyme and which can perform detailed simulations and link bioconversion to upstream fermentation and downstream product purification to determine optimal operating strategies to minimise process costs
additional information
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phylogenetically variant active-site residues are useful for modulating activity of transketolase on natural or structurally-homologous substrates, whereas conserved residues which no longer interact with modified target substrates are useful sites to apply saturation mutagenesis for improvement of activity of transketolase
additional information
ppGpp-dependent functional pathway that operates through transketolase B, and which is buffered in wild-type strain by the presence of an isozyme, transketolase A
additional information
ppGpp-dependent functional pathway that operates through transketolase B, and which is buffered in wild-type strain by the presence of an isozyme, transketolase A
additional information
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ppGpp-dependent functional pathway that operates through transketolase B, and which is buffered in wild-type strain by the presence of an isozyme, transketolase A
additional information
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strategy for identifying target sites for focussed saturation mutagenesis of transketolase, for the incremental modification of substrate specificity. Shell active-site residues that are phylogenetically variant can be randomly mutated to improve the overall activity but not specificity of transketolase. Residues with low sequence entropy that no longer interact with either of the smaller target substrates can similarly provide non-specific activity improvements in at least half of the mutants. The other half of these mutants show a preference for the hydroxylated substrate. Residues with low sequence entropy that interact directly with altered regions of the target substrate are most likely to improve the substrate specificity