Leblová S, Galociová J, Cerovská N
Environ Res. 1983 Apr;30(2):389-92. doi: 10.1016/0013-9351(83)90224-4.
The studied herbicides (terbutylazine, simazine) inhibit the activity of plant, animal, and yeast alcohol dehydrogenases. The inhibition constant Ki for alcohol dehydrogenase (ADH) isolated from peas and bakers' yeast equals approximately 10(-4) M, and that for ADH isolated from horse liver is of the order of 10(-5) M. The character of inhibition for all the herbicides studied for the reaction catalyzed by pea, liver, and yeast ADH is always noncompetitive toward ethanol and competitive with respect to NAD. The inhibition constants for the enzyme isolated from peas are pH independent. The interaction constants found for terbutylazine and simazine and for o-phenanthroline, nicotinamide, and ATP indicate that the herbicides are bonded through the metal component of the enzyme, similar to the nicotinamide part of NAD. The interaction constant less than unity found for the herbicide-ATP system indicates that the bonding site in the active center of the enzyme is different for the herbicides and the adenine part of NAD.
所研究的除草剂（特丁津、西玛津）能抑制植物、动物和酵母的乙醇脱氢酶活性。从豌豆和面包酵母中分离出的乙醇脱氢酶（ADH）的抑制常数Ki约为10^(-4) M，从马肝中分离出的ADH的抑制常数Ki约为10^(-5) M。对于豌豆、肝脏和酵母ADH催化的反应，所研究的所有除草剂的抑制特性对乙醇总是非竞争性的，对NAD是竞争性的。从豌豆中分离出的酶的抑制常数与pH无关。特丁津、西玛津与邻菲罗啉、烟酰胺和ATP的相互作用常数表明，除草剂是通过酶的金属成分结合的，类似于NAD的烟酰胺部分。除草剂 - ATP系统的相互作用常数小于1，表明酶活性中心的结合位点对于除草剂和NAD的腺嘌呤部分是不同的。
