EC Number   |
Application |
Reference |
|---|
    2.2.1.1 | analysis |
a rapid microplate-based approach for measuring the denaturation curves by intrinsic tryptophan fluorescence for simple monomeric and two-state unfolding proteins like transketolase |
691423 |
| 2.2.1.1 | analysis |
coupling of a transketolase reaction that converts D-fructose 6-phosphate to D-erythrose 4-phosphate, which can then be converted to 4-phosphate D-erythronate using erythrose-4-phosphate dehydrogenase, a reaction that reduces NAD+ to NADH and can be easily followed spectrophotometrically |
692925 |
| 2.2.1.1 | analysis |
development of a gas chromatography-based method to screen enzyme activity and stereoselectivity on a wide range of polyol substrates. Method shows reproducibility, sensitivity and range of detection. In combination with HPLC screening, it can be used efficiently to test mutant libraries obtained by directed evolution methods |
721070 |
| 2.2.1.1 | analysis |
establishment of a rapid microplate-based HPLC assay for transketolase, for rapidly determining substrate and product concentration suitable for optimisation of biocatalytic process conditions and screening directed evolution libraries, which can be used to determine transketolase activity with a throughput of up to 1200 samples per day, whereas the well-to-well variation from HPLC measurement is just 1.9% for the lowest activities measured |
691433 |
| 2.2.1.1 | analysis |
highly effective, stable and sensitive method for measuring TKT activity, incorporating xylulokinase, which induces generation of xylulose 5-phosphate from xylulose, from Saccharomyces cerevisiae into conventional TKT assay |
685766 |
| 2.2.1.1 | analysis |
low cost, rapid colorimetric transketolase assay, able to detect value above 8% bioconversion using non-alpha-hydroxylated aldehydes as acceptor substrates. The assay is significantly faster and more convenient to use than HPLC and can be used with a range of aliphatic and aromatic aldehydes. In addition, analysis of the alpha,alpha'-dihydroxyketone produced in the bioconversion can be quantified using this assay system with high-throughput. Furthermore, this method has the potential to be used to screen other chemical reactions or bioconversions leading to the formation of products possessing a 2-hydroxyketone motif |
672550 |
| 2.2.1.1 | analysis |
tetrazolium red-based colorimetric assay to screen for transketolase activity with a range of aldehyde acceptors. The assay is able to detect >8% bioconversion using non-alpha-hydroxylated aldehydes as acceptor substrates and is significantly faster and more convenient to use than chromatographic procedures |
672550 |
| 2.2.1.1 | biotechnology |
improvement of biocatalytic processes using transketolase over prolonged reaction times will need to address the formation of cofactor-associated intermediate state |
692117 |
| 2.2.1.1 | biotechnology |
substrate specificity of transketolase for the donor substrate is broader than expected. Possibility of detecting wild-type transketolase activity in vitro from a L-tyrosine derivative bearing a D-threo ketose, based on the release of L-tyrosine. For cells both auxotrophic for L-tyrosine and expressing transketolase, it shall be possible to carry out this assay in vivo. This strategy may offer the first stereospecific selection test for transketolase mutants |
695175 |
| 2.2.1.1 | drug development |
non-permanently charged thiamine mimetics (thiamine analogs possessing B-rings unable to participate in the cycle) are competent substrates for thiamine pyrophosphokinase, and the resulting pyrophosphates antagonize the activity of transketolase in vitro. Despite remarkable potencies in enzymatic assays, cellular potencies are modest to poor. Inhibition of the thiamine-utilizing enzyme transketolase is linked with diminished tumor cell proliferation |
691299 |
