John C, Lehmann J, Littke W
Carbohydr Res. 1986 Dec 15;158:91-9. doi: 10.1016/0008-6215(86)84008-3.
Two competitive inhibitors of beta-D-galactosidase activity, namely, 2,6-anhydro-S-[ethylmercury(II)]-1-thio-D-glycero-L-manno-heptitol (4) and bis(2,6-anhydro-1-thio-D-glycero-L-manno-heptitol)mercury(II) (6), with inhibition constants of 8.0 X 10(-4) M and 1.9 X 10(-4) M, were synthesized. Compound 6 was incorporated into the crystalline enzyme by cocrystallization. The stoichiometry of the enzyme-inhibitor complex was 1:4, corresponding to one molecule of inhibitor per active site of the enzyme. Compound 4 was found to be unstable against X-ray irradiation, whereas compound 6 was submitted to X-rays for several days without any radiation damage.
合成了两种β-D-半乳糖苷酶活性的竞争性抑制剂，即2,6-脱水-S-[乙基汞（II）]-1-硫代-D-甘油-L-甘露庚糖醇（4）和双（2,6-脱水-1-硫代-D-甘油-L-甘露庚糖醇）汞（II）（6），其抑制常数分别为8.0×10⁻⁴ M和1.9×10⁻⁴ M。通过共结晶将化合物6掺入结晶酶中。酶-抑制剂复合物的化学计量比为1:4，对应于酶的每个活性位点一个抑制剂分子。发现化合物4对X射线照射不稳定，而化合物6在X射线下照射数天未受到任何辐射损伤。
