Results 121 to 130 of about 8,654 (179)
Enzymatic Upgrading of Biomass-Derived Aldoses to Rare Deoxy Ketoses Catalyzed by Transketolase Variants. [PDF]
ChemSusChemArbia G +6 more
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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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Is transketolase-like protein, TKTL1, transketolase?
Biochimica Et Biophysica Acta - Molecular Basis of Disease, 2013 Until recently it was assumed that the transketolase-like protein (TKTL1) detected in the tumor tissue, is catalytically active mutant form of human transketolase (hTKT). Human TKT shares 61% sequence identity with TKTL1. And the two proteins are 77% homologous at the amino acid level.
Olga N Solovjeva, German A Kochetov
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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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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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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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