Journal of Microbiology

Purification and charactedrization of cysteine desulfhydrase from streptomyces albidoflavus SMF301: Ryu, Jae Gon , Kang, Sung Gyun , Kim, In Seop , Rho, Young Taik , Lee, Sang Hee , Lee, Kye Joon; J. Microbiol. 1997;35(2):97-102.

Abstract: Cysteine desulfhydrase (EC 4, 4, 1. 1. ) was purified from the culture supernatant of Streptomyces albidoflavus SMF301 by hydroxyapatite, gel filtration and Resource Q ion-exchange chromatography with a purification fold of six identical subunits. The enzyme was stabilized by dithiothreitol and pyridoxal 5'-phosphate during the purification procedures. The optimum pH and temperature were pH 8.6 and 35℃, respectively. The N-terminal amino acid sequence was identified as A-P-L-P-T-A-D-V-R-S-D-P-G-Y-E-W-L-G-E-A-V. The purified cystein desulfhydrase had a high substrate specificity toward cysteine, and exhibited no cystahionine λ-lyase activity. The K_m value for cysteine was determined to be 0.37 mM.

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