Webb S R, Ferone R
Biochim Biophys Acta. 1976 Feb 13;422(2):419-26. doi: 10.1016/0005-2744(76)90152-2.
Dihydrofolate (H2-folate) synthetase (EC 6.3.2.12) was isolated from Escherichia coli B. A radiochemical assay was developed to determine the activity of H2-folate synthetase in order to study the effects of folate metabolites and antimetabolites which would interfere with the microbiological assay method previously used. The effects of folate and pteroate derivatives on the activity of this enzyme were investigated to determine if inhibition of this enzyme could constitute a site of action for these compounds as chemotherapeutic agents or a site of metabolic regulation. H2-folate synthetase was inhibited by its product, H2-folate, and by the antimetabolite dihydrohomopteroate, with apparent Ki values of 23.4 and 9.2 muM, respectively.
从大肠杆菌B中分离出二氢叶酸（H2 - 叶酸）合成酶（EC 6.3.2.12）。开发了一种放射化学测定法来测定H2 - 叶酸合成酶的活性，以便研究叶酸代谢物和抗代谢物的影响，这些物质会干扰先前使用的微生物测定方法。研究了叶酸和蝶酸衍生物对该酶活性的影响，以确定该酶的抑制是否可能构成这些化合物作为化疗药物的作用位点或代谢调节位点。H2 - 叶酸合成酶受到其产物H2 - 叶酸和抗代谢物二氢高蝶呤的抑制，表观Ki值分别为23.4和9.2 μM。
