Transketolase (abbreviated as TK) is an enzyme that, in humans, is encoded by the TKT gene. (wikipedia.org)
The following human genes encode proteins with transketolase activity: TKT (transketolase) TKTL1 (transketolase-like protein 1) TKTL2 (transketolase-like protein 2) The entrance to the active site for this enzyme is made up mainly of several arginine, histidine, serine, and aspartate side-chains, with a glutamate side-chain playing a secondary role. (wikipedia.org)
These side-chains, to be specific Arg359, Arg528, His469, and Ser386, are conserved within each transketolase enzyme and interact with the phosphate group of the donor and acceptor substrates. (wikipedia.org)
BackgroundPlasmodial transketolase (PTKT) enzyme is one of the novel pharmacological targets being explored as potential anti-malarial drug target due to its functional role and low sequence identity to the human enzyme. (mysciencework.com)
Similar to enzyme crystallins of the lens, both aldehyde dehydrogenase and transketolase are thought to contribute to the optical properties of the cornea. (aao.org)
DXP synthase is a thiamine diphosphate-dependent enzyme related to transketolase and the pyruvate dehydrogenase E1-beta subunit. (nih.gov)
Four major signaling pathways have been implicated in this vascular damage, three of which are activated by increased availability of the glycolytic metabolites produced by the thiamine-dependent enzyme transketolase. (the-scientist.com)
It does this by blocking a key thiamine-dependent enzyme called transketolase. (hormonesmatter.com)
There is some research that suggesting that it blocks the pyruvate dehydrogenase enzyme in advance of blocking transketolase, but this seems less well investigated. (hormonesmatter.com)
Transketolase is cytosolic enzyme with an oxidative and non-oxidative branch that connects aerobic anaerobic metabolism through something called the pentose phosphate pathway (PPP). (hormonesmatter.com)
Wernicke-Korsakoff syndrome Symptoms and Signs is caused by a partial deficiency of transketolase, which is an enzyme for the pentose phosphate pathway that requires thiamin as a cofactor. (merckmanuals.com)
Thiamine pyrophosphate1
A stimulation of over 20%-25% during a red blood cell transketolase measurement using thiamine pyrophosphate (TTP) indicates deficiency. (medscape.com)
Pentose phospha1
In mammals, transketolase connects the pentose phosphate pathway to glycolysis, feeding excess sugar phosphates into the main carbohydrate metabolic pathways. (wikipedia.org)
Erythrocyte4
Protocol and application of basal erythrocyte transketolase activity to improve assessment of thiamine status. (mysciencework.com)
The erythrocyte transketolase activity coefficient (ETKac) is a sensitive measure of thiamine status, but its interpretation may be co. (mysciencework.com)
Erythrocyte transketolase activity coefficient (ETKAC) assay protocol for the assessment of thiamine status. (mysciencework.com)
Erythrocyte transketolase activity is lower in nondialyzed patients than in dialyzed patients. (medscape.com)
Industrial Biotechnology1
Engineering Transketolase for Industrial Biotechnology. (ucl.ac.uk)
Crystallins1
Transketolase is abundantly expressed in the mammalian cornea by the stromal keratocytes and epithelial cells and is reputed to be one of the corneal crystallins. (wikipedia.org)
Phosphorylation2
DFA mimics ribose in vivo and accumulates in cells following phosphorylation by ribokinase and further metabolism by transketolase. (ca.gov)
Calcium regulation in chloroplasts and the role of calcium-dependent phosphorylation of transketolase in carbon metabolism. (uni-muenchen.de)
Assay1
A functional enzymatic assay of transketolase activity measured before and after the addition of TTP is a more reliable way to measure thiamine nutritional status. (medscape.com)
Activity2
This novel reconstituted transketolase is thermally stable with no loss of activity after incubation for 1 h at 70°C and is stable after 1 h incubation with 50% of the organic solvents methanol, ethanol, isopropanol, DMSO, acetonitrile and acetone. (rcsb.org)
evaluated the effect of benfotiamine on transketolase activity in both cultured endothelial cells and animal tissues. (the-scientist.com)
Reaction1
Moreover, in the Calvin cycle this is the first reaction catalyzed by transketolase, rather than the second. (wikipedia.org)
Catalyzes2
Transketolase catalyzes two important reactions, which operate in opposite directions in these two pathways. (wikipedia.org)
Human transketolase (TKT, EC 2.2.1.1) catalyzes transfers two-carbon units from ketoses (donor) to aldoses (acceptor). (alliedacademies.org)
Effect1
This also abolished the counteracting effect of sulforaphane, suggesting mediation by nrf2 and related increase of transketolase expression. (diabetesjournals.org)
Human1
Human corneas possess a remarkably high level of aldehyde dehydrogenase and transketolase. (aao.org)
Results2
Overexpression of Plastid Transketolase in Tobacco Results in a Thiamine Auxotrophic Phenotype. (mpg.de)
RESULTS- Activation of nrf2 by sulforaphane induced nuclear translocation of nrf2 and increased ARE-linked gene expression, for example, three- to fivefold increased expression of transketolase and glutathione reductase. (diabetesjournals.org)
Search1
Search Transketolase as keywords on MyScienceWork's publications. (mysciencework.com)
Role1
CONCLUSIONS- We conclude that activation of nrf2 may prevent biochemical dysfunction and related functional responses of endothelial cells induced by hyperglycemia in which increased expression of transketolase has a pivotal role. (diabetesjournals.org)
Erythrocyte8
The primary outcome measure was 15% change in erythrocyte transketolase activity (ETKA) in group 3. (nature.com)
Comparison of Thiamin Diphosphate High-Performance Liquid Chromatography and Erythrocyte Transketolase Assays for Evaluating Thiamin Status in Malaria Patients without Beriberi. (tropmedres.ac)
Thiamin status has traditionally been measured through the erythrocyte activation assay (ETKA) or basal transketolase activity (ETK), which indirectly measure thiamin diphosphate (TDP). (tropmedres.ac)
The method used to estimate the Recommended Dietary Allowance ( RDA ) for thiamin combines erythrocyte transketolase activity, urinary thiamin excretion, and other findings. (nih.gov)
Measuring whole blood or erythrocyte transketolase activity, with and without addition of thiamine diphosphate, is the most reliable method of detecting thiamine deficiency (9). (cdc.gov)
Erythrocyte transketolase activity is lower in nondialyzed patients than in dialyzed patients. (medscape.com)
Thiamin status is often measured indirectly by assaying the activity of the transketolase enzyme, which depends on TDP, in erythrocyte hemolysates in the presence and absence of added TDP [ 3 ]. (nih.gov)
studies have shown a higher risk of thiamin deficiency in people with type 1 and/or type 2 diabetes based on tests of erythrocyte transketolase activity. (wonderlabs.com)
Wernicke-Korsakof1
I was trained as a graduate student by Charles Singleton with Peter Martin studying the genetics of alcoholism focusing the contributions of the thiamine-requiring enzyme transketolase in the development of Wernicke-Korsakoff syndrome in human alcoholics. (wakehealth.edu)
Enzyme transketolase2
Thiamine and magnesium also serve as co-factors for the cytoplasmic enzyme, transketolase (TK), which catalyses the reversible arm of the Pentose Phosphate Pathway (PPP). (nature.com)
May be more effective in controlling damage from diabetes because it is a better activator of the enzyme transketolase. (psychologicalharassment.com)
Thiamine Pyrophosphate1
Thiamine (as thiamine pyrophosphate) is important in carbohydrate and amino acid metabolism, forming an essential component of 2-oxoacid dehydrogenases (including pyruvate dehydrogenase and branched chain oxoacid dehydrogenase) and transketolase. (vin.com)
TKL11
Five target proteins were successfully purified from yeast whole cell extract: Transketolase (TKL1), inorganic pyrophosphatase (IPP1), amidotransferase/cyclase HIS7, phosphoglycerate kinase (PGK1) and enolase (ENO1). (uwaterloo.ca)
TKTL13
The following human genes encode proteins with transketolase activity: TKT (transketolase) TKTL1 (transketolase-like protein 1) TKTL2 (transketolase-like protein 2) The entrance to the active site for this enzyme is made up mainly of several arginine, histidine, serine, and aspartate side-chains, with a glutamate side-chain playing a secondary role. (wikipedia.org)
B-MYB (or MYBL2), Cancerous Inhibitor of PP2A (CIP-2a), and transketolase-like1 (TKTL1). (frontiersin.org)
after transfection with anti-TKTL1 siRNA, total transketolase activity dramatically decreases and proliferation was significantly inhibited in cancer cells. (nih.gov)
Cofactor1
It's also a cofactor to several enzymes that help metabolize carbohydrates, including transketolase and branched-chain α-keto acid dehydrogenase. (purebulk.com)
Compounds1
Transketolase helps in keeping glucose-derived compounds out of blood vessels and nerve cells. (psychologicalharassment.com)
Molecule1
The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site. (nih.gov)
Gene1
Transketolase (abbreviated as TK) is an enzyme that, in humans, is encoded by the TKT gene. (wikipedia.org)
Enzymes1
In a second case, John Ward of University College London has shown that transketolases and transaminases can be used in a cascade to produce chiral amino diols, and by carrying the different enzymes, all four enantiomers of these ketodiols can be made. (manufacturingchemist.com)
Group1
These side-chains, to be specific Arg359, Arg528, His469, and Ser386, are conserved within each transketolase enzyme and interact with the phosphate group of the donor and acceptor substrates. (wikipedia.org)