Enzymatic synthesis of l-cystathionine from the succinic ester of l-homoserine

Abstract

The product of the reaction between l-cysteine and O- succinyl- l - homoserine , catalyzed by an enzyme from Salmonella, has been shown to be l-cystathionine. The three times recrystallized reaction product and authentic l-cystathionine have identical infrared spectra and optical-rotary dispersion curves, are decomposed at equal rates by a 100-fold purified cystathionine β-cleavage enzyme from Escherichia coli, have the same R F 's on paper chromatography and are both desulfurated by Raney nickel into l-alanine and l-α-aminobutyric acid.