Results 121 to 130 of about 8,762 (179)

Extensive richness and novel taxa of sulfoquinovose-degrading bacteria in the cow rumen

open access: yes
Krasenbrink J   +15 more
europepmc   +1 more source

Structure and functioning mechanism of transketolase

Biochimica Et Biophysica Acta - Proteins and Proteomics, 2014
Studies 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 ...
Olga N Solovjeva, German A Kochetov
exaly   +3 more sources

Substrate inhibition of transketolase

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2016
We 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
openaire   +2 more sources

The affinity chromatography of transketolase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1978
A 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
openaire   +2 more sources

The electrophoresis and detection of transketolase

Analytical Biochemistry, 1981
Abstract 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
openaire   +2 more sources

Transketolase in Trypanosoma brucei

Molecular and Biochemical Parasitology, 2011
A 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
openaire   +3 more sources

Improving Transketolase

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
openaire   +1 more source

Inhibition of transketolase by hexacyanoferrate(III)

Biochemistry (Moscow), 2010
The 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
openaire   +2 more sources

The Catalytic Mechanism of Human Transketolase

ChemPhysChem, 2019
AbstractWe have computationally determined the catalytic mechanism of human transketolase (hTK) using a cluster model approach and density functional theory calculations. We were able to determine all the relevant structures, bringing solid evidences to the proposed experimental mechanism, and to add important detail to the structure of the transition ...
Prejano M.   +5 more
openaire   +2 more sources

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