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Applied Microbiology and Biotechnology, 2008
The alcohol dehydrogenase from Thermus sp. ATN1 (TADH) was characterized biochemically with respect to its potential as a biocatalyst for organic synthesis. TADH is a NAD(H)-dependent enzyme and shows a very broad substrate spectrum producing exclusively the (S)-enantiomer in high enantiomeric excess (>99%) during asymmetric reduction of ketones.
Frank Hollmann, Andreas Schmid
exaly +4 more sources
The alcohol dehydrogenase from Thermus sp. ATN1 (TADH) was characterized biochemically with respect to its potential as a biocatalyst for organic synthesis. TADH is a NAD(H)-dependent enzyme and shows a very broad substrate spectrum producing exclusively the (S)-enantiomer in high enantiomeric excess (>99%) during asymmetric reduction of ketones.
Frank Hollmann, Andreas Schmid
exaly +4 more sources
Cloning and expression of a tauropine dehydrogenase from the marine sponge Suberites domuncula
Marine Biology, 2008Bruna Plese, Werner E G Müller
exaly
Chlorophyll accumulation is enhanced by osmotic stress in graminaceous chlorophyllic cells
Journal of Plant Physiology, 2005Quintin Rascon-Cruz +1 more
exaly

