Kwon K S, Hah Y C, Hong S W
Department of Microbiology, College of Natural Sciences, Seoul National University, Korea.
Microbios. 1988;54(220-221):149-56.
The location and biosynthetic regulation of endo-1,4-beta-glucanase were studied in Aspergillus nidulans. The enzyme was found to be extracellular, but low intracellular activity was also detected at the beginning of enzyme induction. The synthesis of the enzyme was regulated by carbon catabolite repression as well as specific induction. beta-1,4-Linked carbohydrates, such as carboxymethylcellulose, cellobiose and lactose, induced the enzyme synthesis, while 2-deoxyglucose and readily metabolizable substrates, such as glucose and glycerol, repressed it. Carbon catabolite repression could not be overcome by cAMP. Actinomycin D and cycloheximide completely inhibited the enzyme synthesis, which indicated the novo synthesis.
对构巢曲霉中内切 - 1,4 - β - 葡聚糖酶的定位及生物合成调控进行了研究。发现该酶是胞外酶,但在酶诱导初期也检测到了低水平的细胞内活性。该酶的合成受碳分解代谢物阻遏以及特异性诱导的调控。β - 1,4 - 连接的碳水化合物,如羧甲基纤维素、纤维二糖和乳糖,可诱导该酶的合成,而2 - 脱氧葡萄糖以及易于代谢的底物,如葡萄糖和甘油,则会抑制其合成。环磷酸腺苷(cAMP)无法克服碳分解代谢物阻遏。放线菌素D和环己酰亚胺完全抑制了该酶的合成,这表明是从头合成。