A phosphinic analogue of methionine is a substrate of L-methionine-γ-lyase and induces the synthesis of the enzyme in Citrobacter intermedius cells

Chemoenzymatic synthesis of optically active phosphinic analogues of S-substituted sulfur-containing amino acids

“…This reaction was also possible for analogue 1, whose interaction with benzylthiol under the action of Citrobacter intermedius cells containing L-methionine-γ-lyase afforded optically active acid 2, although with a low yield. 8 We examined various conditions of the enzymatic synthesis of compound 2 from acid 1 and benzylthiol and found that the use of L-methionine-γ-lyase ‡ instead of intact cells as a biocatalyst allowed us to increase the yield of 2 up to 45%. § The (R)-configuration was ascribed to optically active acid 2 based on that the stereochemistry of the enzymatic reaction remains the same on going from the natural substrate to its phosphinic analogue, as it was observed for the reaction of L-tyrosinephenol-lyase with the enantiomers of tyrosine phosphinic analogues.…”

“…6 ‡ L-Methionine-γ-lyase was obtained from C. intermedius cells according to a published procedure. 8 The activity of the preparation was assayed by measuring the rate of α-ketobutyrate formation from L-methionine according to Friedemann. 9 One unit of enzymic activity was determined as the enzyme amount catalysing the transformation of 1 µmol of L-methionine per minute at 30 °C and a 40 mM concentration of L-methionine.…”