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Properties and functions of the thiamin diphosphate dependent enzyme transketolase
International Journal of Biochemistry and Cell Biology, 1998 This review highlights recent research on the properties and functions of the enzyme transketolase, which requires thiamin diphosphate and a divalent metal ion for its activity.
Gerhard Schenk +2 more
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Molecular Evolutionary Analysis of the Thiamine-Diphosphate-Dependent Enzyme, Transketolase [PDF]
Journal of Molecular Evolution, 1997 Members of the transketolase group of thiamine- diphosphate-dependent enzymes from 17 different organisms including mammals, yeast, bacteria, and plants have been used for phylogenetic reconstruction. Alignment of the amino acid and DNA sequences for
Gerhard Schenk +2 more
exaly +3 more sources
British Journal of Cancer, 2006 Tumours ferment glucose to lactate even in the presence of oxygen (aerobic glycolysis; Warburg effect). The pentose phosphate pathway (PPP) allows glucose conversion to ribose for nucleic acid synthesis and glucose degradation to lactate.
F Willeke, G Stassi, Weiss C
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Substrate inhibition of transketolase
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2016We studied the influence of the acceptor substrate of transketolase on the activity of the enzyme in the presence of reductants. Ribose-5-phosphate in the presence of cyanoborohydride decreased the transketolase catalytic activity. The inhibition is caused by the loss of catalytic function of the coenzyme-thiamine diphosphate. Similar inhibitory effect
Olga N, Solovjeva +2 more
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The affinity chromatography of transketolase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1978A number of possible affinity adsorbents for transketolase (sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphateglycolaldehydetransferase, EC 2.2.1.1) were prepared. The behaviour of the enzyme from Candida utilis and from Baker's yeast on columns of these and of Blue Sepharose CL-6B was examined, together with the behaviour of the contaminating ...
T, Wood, S, Fletcher
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The electrophoresis and detection of transketolase
Analytical Biochemistry, 1981Abstract After electrophoresis impure transketolase preparations stained readily with an activity stain based on a published method, but pure preparations gave no reaction. The bands first obtained were due to the presence of (i) a transketolase- d -glyceraldehyde-3-phosphate dehydrogenase complex, (ii) alcohol dehydrogenases, and (iii) a zone of ...
T, Wood, C C, Muzariri
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Topics in Catalysis, 2013
Transketolase is an enzyme catalysing asymmetric C–C bond formation which is of great interest for many syntheses of biologically active compounds. Enzymatic couplings present many advantages (mild reaction conditions notably), nonetheless their utilisation on an industrial scale is often limited by restricting factors as their activity, substrate ...
Adeline Ranoux, Ulf Hanefeld
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Transketolase is an enzyme catalysing asymmetric C–C bond formation which is of great interest for many syntheses of biologically active compounds. Enzymatic couplings present many advantages (mild reaction conditions notably), nonetheless their utilisation on an industrial scale is often limited by restricting factors as their activity, substrate ...
Adeline Ranoux, Ulf Hanefeld
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Structure and functioning mechanism of transketolase
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2014Studies of thiamine diphosphate-dependent enzymes appear to have commenced in 1937, with the isolation of the coenzyme of yeast pyruvate decarboxylase, which was demonstrated to be a diphosphoric ester of thiamine. For quite a long time, these studies were largely focused on enzymes decarboxylating α-keto acids, such as pyruvate decarboxylase and ...
German A, Kochetov, Olga N, Solovjeva
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Inhibition of transketolase by hexacyanoferrate(III)
Biochemistry (Moscow), 2010The effect of hexacyanoferrate(III) on the catalytic activity of transketolase has been studied. This oxidant inactivates only one of two active sites of the enzyme, the one with a higher affinity to the coenzyme (thiamine diphosphate). The second active site does not lose its catalytic activity.
V A, Yurshev +3 more
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Sulfhydryl groups and transketolase activity
Biochemical and Biophysical Research Communications, 1966Abstract Transketolase, an enzyme of pentose cycle, catalyzes the reaction of glycolaldehyde transport from the xylulose-5-phosphate to the ribose-5-phosphate with the formation of sedoheptulose-7-phosphate. There is not much known about this enzyme, especially in respect to its functional groups.
G A, Kochetov, F G, Lutovinova
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