Meisch H U, Kappesser S
Biochim Biophys Acta. 1987 Aug 13;925(2):234-7. doi: 10.1016/0304-4165(87)90114-0.
Vanadate stimulates the liberation of H2S from cysteine in intact cells of baker's yeast (Saccharomyces cerevisiae) with a maximal increase of 60% at 10 microM NH4VO3. Protein separation from crude yeast extract yielded two active protein fractions which were found to catalyze the degradation of cysteine to H2S, pyruvate and ammonia or H2S and serine, respectively, thus characterizing them as cysteine desulphydrase and serine sulphydrase. Only the latter enzyme was found to be activated by vanadate, showing optimal enhancement of about 100% at 10 microM NH4VO3.
钒酸盐能刺激面包酵母(酿酒酵母)完整细胞中半胱氨酸释放硫化氢,在10微摩尔偏钒酸铵存在时,硫化氢释放量最大可增加60%。从粗酵母提取物中分离蛋白质得到两个活性蛋白组分,发现它们分别催化半胱氨酸降解为硫化氢、丙酮酸和氨,或硫化氢和丝氨酸,因此将它们分别鉴定为半胱氨酸脱硫酶和丝氨酸巯基酶。结果发现只有后一种酶能被钒酸盐激活,在10微摩尔偏钒酸铵存在时,活性最佳增强约100%。