Dunlop P C, Roon R J
J Bacteriol. 1975 Jun;122(3):1017-24. doi: 10.1128/jb.122.3.1017-1024.1975.
During recent studies conducted with suspensions of three strains of Saccharomyces cerevisiae, it was observed that ammonia was rapidly liberated when L-asparagine was added to the medium. Subsequent investigation has revealed that these strains of S. cerevisiae have an externally active asparaginase as well as an internally active one. The appearance of the external asparaginase is stimulated by nitrogen starvation, requires an available energy source, and is prevented by cycloheximide. The internal enzyme appears to be constitutive. The external activity is relatively insensitive to para-hydroxymercuribenzoate inhibition, whereas the internal activity is highly inhibited by this compound.
在最近对三株酿酒酵母菌株的悬浮液进行的研究中,观察到当向培养基中添加L-天冬酰胺时,氨会迅速释放出来。随后的研究表明,这些酿酒酵母菌株既有一种胞外活性天冬酰胺酶,也有一种胞内活性天冬酰胺酶。胞外天冬酰胺酶的出现受到氮饥饿的刺激,需要有可用的能量来源,并且会被环己酰亚胺抑制。胞内酶似乎是组成型的。胞外活性对对羟基汞苯甲酸的抑制相对不敏感,而胞内活性则受到该化合物的高度抑制。