Title Purification and charactedrization of cysteine desulfhydrase from streptomyces albidoflavus SMF301
Author Ryu, Jae Gon · Kang, Sung Gyun · Kim, In Seop · Rho, Young Taik · Lee, Sang Hee · Lee, Kye Joon *
Address Department of Microbiology, College of Natural Sciences, Seoul National University
Bibliography Journal of Microbiology, 35(2),97-102, 1997,
Key Words Cysteine desulfhydrase, Streptomyces, purification, N-terminal sequence
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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