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Extensive richness and novel taxa of sulfoquinovose-degrading bacteria in the cow rumen
Krasenbrink J +15 more
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Ecological success in freshwater lakes: insights from novel cultivated lineages of the abundant Nanopelagicales order. [PDF]
Chiriac MC +25 more
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Effect of xylitol on low‑density lipoprotein‑stimulated oxidative stress in THP‑1 cells. [PDF]
Huang Z +8 more
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Genetic Variants Influence the Development of Diabetic Neuropathy. [PDF]
Hajdú N +8 more
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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
openaire +1 more source
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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Transketolase in Trypanosoma brucei
Molecular and Biochemical Parasitology, 2011A single copy gene, encoding a protein highly similar to transketolase from other systems, was identified in the Trypanosoma brucei genome. The gene was expressed in E. coli and the purified protein demonstrated transketolase activity with K(m) values of 0.2mM and 0.8mM respectively for xylulose 5-phosphate and ribose 5-phosphate.
Stoffel, Sabine A. +7 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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