• Journal of Microbiology
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• 제35권2호
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• pp.97-102
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• 1997

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$^{\circ}C$, respectively. The N-terminal amino acid sequence was identified as A-P-L-P-T-A-D-V-R-S-D-P-G-Y-R-E-W-L-G-E-A-V. The purified cystein desulfhydrase had a high substrate specificity toward cysteine, and exhibited no cystahionine $\gamma$-lyase activity. The $K_m$ value for cysteine was determined to be 0.37 mM.