Purification and Charactedrization of Cysteine Desulfhydrase from Streptomyces albidoflavus SMF301

  • Ryu, Jae-Gon (Department of Microbiology, Seoul National University) ;
  • Kang, Sung-Gyun (Department of Microbiology, Seoul National University) ;
  • Kim, In-Seop (Department of Microbiology, Seoul National University) ;
  • Rho, Young-Taik (Department of Microbiology, Seoul National University) ;
  • Lee, Sang-Hee (Department of Microbiology, Seoul National University) ;
  • Lee, Kye-Joon (Department of Microbiology, Seoul National University)
  • Published : 1997.06.01

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$^{\circ}C$, 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.

Keywords

References

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