Stereospecific abstraction of epsilon-pro-R-hydrogen of L-lysine by L-lysine epsilon-dehydrogenase from Agrobacterium tumefaciens |
| |
Authors: | H Misono T Yoshimura S Nagasaki K Soda |
| |
Institution: | Department of Agricultural Chemistry, Kochi University. |
| |
Abstract: | The stereochemical aspects of the L-lysine epsilon-dehydrogenase reaction were examined with (6R)-L-6-3H]lysine and (6S)-DL-6-3H]lysine. When (6S)-DL-6-3H]lysine was used as a substrate, the tritium was found in the product, delta 1-piperideine-6-carboxylate. In contrast, the radioactivity from (6R)-L-6-3H]lysine was not retained in the product. Thus, the pro-R hydrogen at the prochiral C-6 carbon of L-lysine is specifically abstracted by the enzyme: the enzyme behaves stereochemically as an amino acid D-dehydrogenase. |
| |
Keywords: | |
|
|