Purification, characterization and identification of cysteine desulfhydrase of Corynebacterium glutamicum, and its relationship to cysteine production

Abstract

We highly purified the enzyme having L-cysteine desulfhydrase activity from Corynebacterium glutamicum. According to its partial amino acid sequence, the enzyme was identified as the aecD gene product, a C-S lyase with alpha, beta-elimination activity [I. Rossol and A. Pühler (1992) J. Bacteriol. 174, 2968-2977]. To produce L-cysteine in C. glutamicum, the Escherichia coli-altered cysE gene encoding Met256Ile mutant serine acetyltransferase, which is desensitized to feedback inhibition by L-cysteine, was introduced into C. glutamicum. When the altered cysE gene was expressed in the aecD-disrupted strain, the transformants produced approximately 290 mg of L-cysteine plus L-cystine per liter from glucose. The produced amount of these amino acids was about two-fold higher than that of the wild-type strain.