Hsu Y P, Kohlhaw G B, Niederberger P
J Bacteriol. 1982 May;150(2):969-72. doi: 10.1128/jb.150.2.969-972.1982.
The specific activity and the immunoreactive amount of alpha-isopropylmalate synthase were more than three times above wild-type values in a Saccharomyces cerevisiae mutant (cdr1) with constitutively derepressed levels of enzymes known to be under the "general" control of amino acid biosynthesis. The specific activity was also higher in lysine- and arginine-leaky strains when these were grown under limiting conditions, and in wild-type cells grown in the presence of 5-methyltryptophan. A low specific activity was found in a mutant (ndr1) unable to derepress enzymes of the general control system. Neither isopropylmalate isomerase nor beta-isopropylmalate dehydrogenase responded to general control signals.
在酿酒酵母突变体(cdr1)中,α-异丙基苹果酸合酶的比活性和免疫反应量比野生型值高出三倍多,该突变体中已知受氨基酸生物合成“一般”控制的酶水平持续去阻遏。当赖氨酸和精氨酸渗漏菌株在限制条件下生长时,以及野生型细胞在5-甲基色氨酸存在下生长时,比活性也较高。在一个无法去阻遏一般控制系统酶的突变体(ndr1)中发现比活性较低。异丙基苹果酸异构酶和β-异丙基苹果酸脱氢酶均不响应一般控制信号。