Meitinger N, Munkert J, Maia de Pádua R, De Souza Filho JD, Maid H, Bauer W, Braga FC, Kreis W (2016)
Publication Language: English
Publication Type: Journal article, Original article
Publication year: 2016
Publisher: Elsevier
Book Volume: 57
Pages Range: 1567-1571
Journal Issue: 14
DOI: 10.1016/j.tetlet.2016.02.099
Studies indicate that the isomerization catalyzed by the Dl3KSI proceeds without significant isotope exchange between the medium and the steroid and thus involves an intramolecular proton transfer consistent with the mechanism of the bacterial 3-ketosteroid isomerase of Pseudomonas testosteroni. For the rDl3 beta HSD as well as under non-enzymatic conditions deuterium was incorporated from the incubation buffer during isomerization. Together with a comparison of the rate of isomerization under the different conditions, it was demonstrated that rDl3 beta HSD does not possess 3-ketosteroid isomerase activity. (C) 2016 Elsevier Ltd. All rights reserved.
APA:
Meitinger, N., Munkert, J., Maia de Pádua, R., De Souza Filho, J.D., Maid, H., Bauer, W.,... Kreis, W. (2016). The catalytic mechanism of the 3-ketosteroid isomerase of Digitalis lanata involves an intramolecular proton transfer and the activity is not associated with the 3 beta-hydroxysteroid dehydrogenase activity. Tetrahedron Letters, 57(14), 1567-1571. https://dx.doi.org/10.1016/j.tetlet.2016.02.099
MLA:
Meitinger, Nadine, et al. "The catalytic mechanism of the 3-ketosteroid isomerase of Digitalis lanata involves an intramolecular proton transfer and the activity is not associated with the 3 beta-hydroxysteroid dehydrogenase activity." Tetrahedron Letters 57.14 (2016): 1567-1571.
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