Kumar V, Maresca B, Sacco M, Goewert R, Kobayashi G S, Medoff G
Biochemistry. 1983 Feb 15;22(4):762-8. doi: 10.1021/bi00273a009.
A cysteine dioxygenase, cysteine oxidase (EC 1.13.11.20), has been purified from the cytosolic fraction of yeast phase cells of the dimorphic fungus Histoplasma capsulatum. The cysteine oxidase is an iron-containing dioxygenase with a molecular weight of 10500 (+/- 1500) and is present only in the yeast phase of the fungus. The enzyme is highly specific for L-cysteine, with a Km of 2 X 10(-5) M in vitro. The product of cysteine oxidation is cysteinesulfinic acid, as analyzed by thin-layer chromatography and mass spectroscopy. To our knowledge, this is the first cysteine oxidase isolated from a fungus, and it probably plays an important role in the mycelial to yeast phase transition of H. capsulatum during which redox potential and cysteine levels are crucial factors.
已从二态真菌荚膜组织胞浆菌酵母相细胞的胞质部分中纯化出一种半胱氨酸双加氧酶,即半胱氨酸氧化酶(EC 1.13.11.20)。该半胱氨酸氧化酶是一种含铁双加氧酶,分子量为10500(±1500),且仅存在于该真菌的酵母相中。该酶对L-半胱氨酸具有高度特异性,体外Km值为2×10⁻⁵ M。通过薄层色谱和质谱分析,半胱氨酸氧化的产物为半胱亚磺酸。据我们所知,这是首次从真菌中分离出的半胱氨酸氧化酶,它可能在荚膜组织胞浆菌从菌丝体向酵母相转变过程中发挥重要作用,在此过程中氧化还原电位和半胱氨酸水平是关键因素。