Stereospecific abstraction of epsilon-pro-R-hydrogen of L-lysine by L-lysine epsilon-dehydrogenase from Agrobacterium tumefaciens.
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.
Misono
H
H
Department of Agricultural Chemistry, Kochi University.
Yoshimura
T
T
Nagasaki
S
S
Soda
K
K
D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism*; D012231:Rhizobium / Q000201:enzymology*; D013237:Stereoisomerism; D013379:Substrate Specificity
D000594:Amino Acid Oxidoreductases; C034168:lysine epsilon-dehydrogenase; D008239:Lysine