Enzymic and chemical synthesis of epilson-N-(L-propionyl-2)-L-lysine.
Pyruvate was shown to act as an oxo acid substrate in the reverse direction of saccharopine dehydrogenase [epsilon N-(L-glutaryl-2)-L-lysine: NAD oxidoreductase (L-lysine-forming)] reaction. The enzymic condensation product of lysine and pyruvate was isolated and identified as epsilon-N-(L-propionyl-2)-L-lysine by comparison with the synthetic compound. A method for the chemical preparation of diastereoisomers of epsilon-N-(propionyl-2)-L-lysine is also described.
D008239:Lysine / Q000031:analogs & derivatives* / Q000096:biosynthesis / Q000138:chemical synthesis; D009682:Magnetic Resonance Spectroscopy; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism*; D011773:Pyruvates; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D012443:Saccharopine Dehydrogenases / Q000378:metabolism*; D013055:Spectrophotometry, Infrared
D011773:Pyruvates; D000587:Oxidoreductases Acting on CH-NH Group Donors; D012443:Saccharopine Dehydrogenases; D008239:Lysine