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
-
glycation
- encephalopathy
- pyridoxine
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apoenzyme
- phosphoglycerate
- wernicke
-
baker
- oxythiamine
- neuropathy
- ribose-5-phosphate
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thiamine-deficient
- xylulose
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thiamine-dependent
- 6-phosphogluconate
- riboflavin
-
calvin
- pharmacology
- drug development
- biotechnology
-
pentose-phosphate
- xylulokinase
- industry
- alpha-ketoglutarate
- dihydroxyacetone
-
warburg
- phosphoketolase
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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
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
ECTree
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Cofactor
Cofactor on EC 2.2.1.1 - transketolase
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additional information
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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
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thiamine diphosphate
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thiamine diphosphate
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not thiamine, thiamine mono-or triphosphate
thiamine diphosphate
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negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+
thiamine diphosphate
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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
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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
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interaction with the coenzyme binding site of the enzyme is described
thiamine diphosphate
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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
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thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium
thiamine diphosphate
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form
thiamine diphosphate
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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
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homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel
thiamine diphosphate
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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
thiamine diphosphate
an active site cleft is formed between the two monomeric units allowing the cofactors thiamine diphosphate and Mg2+ to bind, such that the N-terminal domain I of chain A binds the diphosphate moiety of thiamine diphosphate, and domain II of chain B interacts with the aminopyrimidine ring. The diphosphate moiety of thiamine diphosphate is anchored in place through a number of hydrogen bonds formed with residues Thr48, His85, Ser176, Asp177, Gly178, Asn207, Ile209 and His283 from one monomer, crystallization data
thiamine diphosphate
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate