Coukell M B, Polglase W J
Biochem J. 1969 Feb;111(3):273-8. doi: 10.1042/bj1110273.
Acetolactate formation in Escherichia coli B results from the activity of a single system, acetohydroxy acid synthetase, which has a pH optimum of 8.0 and is sensitive to end-product inhibition by l-valine. Acetohydroxy acid synthetase was found to be subject to catabolite repression, and the nature and concentration of the carbon source had a greater effect on the formation of the enzyme than had the known end products (valine, isoleucine, leucine and pantothenate) of the biosynthetic pathways of which this enzyme is a member. The results suggest that acetohydroxy acid synthetase may play an amphibolic role in E. coli B.
大肠杆菌B中乙酰乳酸的形成源于单一系统——乙酰羟酸合成酶的活性,该酶的最适pH值为8.0,且对L-缬氨酸的终产物抑制敏感。发现乙酰羟酸合成酶受分解代谢物阻遏,与该酶所属生物合成途径的已知终产物(缬氨酸、异亮氨酸、亮氨酸和泛酸盐)相比,碳源的性质和浓度对该酶形成的影响更大。结果表明,乙酰羟酸合成酶可能在大肠杆菌B中发挥兼性代谢作用。