Schirmeister T
Institute for Pharmacy and Food Chemistry, University of Würzburg, Germany.
Bioorg Med Chem Lett. 2000 Dec 4;10(23):2647-51. doi: 10.1016/s0960-894x(00)00549-7.
For (S)-thiirancarboxylic acid a second-order rate constant of k2nd = 222 M(-1) min(-1) for the irreversible inhibition of papain was determined. The ethyl and methyl ester do not inhibit the enzyme time-dependently. An improved synthesis of enantiomerically pure thiirancarboxylic acid is described. It is shown that thiirancarboxylates can be substrates for serine proteases (alpha-chymotrypsin) and esterases (pig liver esterase) and even for metallo proteases (thermolysin).
对于（S）-硫代环丙烷羧酸，测定了其对木瓜蛋白酶不可逆抑制的二级速率常数k2nd = 222 M⁻¹ min⁻¹。乙酯和甲酯不会随时间依赖性地抑制该酶。描述了对映体纯硫代环丙烷羧酸的改进合成方法。结果表明，硫代环丙烷羧酸盐可以作为丝氨酸蛋白酶（α-胰凝乳蛋白酶）、酯酶（猪肝酯酶）甚至金属蛋白酶（嗜热菌蛋白酶）的底物。
