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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

Reaction

sedoheptulose 7-phosphate
+
D-glyceraldehyde 3-phosphate
=
D-ribose 5-phosphate
+
D-xylulose 5-phosphate

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

     2 Transferases
         2.2 Transferring aldehyde or ketonic groups
             2.2.1 Transketolases and transaldolases
                2.2.1.1 transketolase

Inhibitors

Inhibitors on EC 2.2.1.1 - transketolase

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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
2-[(2,2-dimethyl-2,3-dihydro-1-benzofuran-7-yl)oxy]-N-[1-(4-ethyl-6-hydroxypyrimidin-2-yl)-4-(furan-2-yl)-1H-pyrrol-2-yl]acetamide
-
-
3-(2,4-dichlorophenoxy)-N-[3-(furan-2-yl)-1-(pyrimidin-2-yl)-1H-pyrazol-5-yl]propanamide
-
-
3-(6-methyl-2-amino-pyridin-3-ylmethyl)-5-(2-hydroxy-ethyl)-4-methyl-thiazol-3-ium chloride hydrochloride
3-formylbenzoic acid
-
substrate inhibition
4'-methylamino-thiamine diphosphate
-
cofactor analogue
alpha-terthienyl
-
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
N-[1-(3-chloro-5-methylpyridin-2-yl)-3-(furan-2-yl)-1H-pyrazol-5-yl]-3-phenoxypropanamide
-
-
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
oxidized dithiothreitol
in the absence of Mg2+, the enzyme is strongly inhibited by oxidation, retaining 20-30 % of its control activity when exposed to 50 mM oxidized dithiothreitol. The apoenzyme is 80% inactivated following incubation in the presence of identical amount of oxidized dithiothreitol
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
ZINC12007063
-
i.e. 2-[(2,2-dimethyl-3H-benzofuran-7-yl)oxy]-N-[2-(4-ethyl]-6-oxo-1H-pyrimidin-2-yl)-5-(2-furyl)pyrazol-3
additional information
-