利什曼原虫中存在功能性乙醛酸循环的证据。
Evidence for a functional glyoxylate cycle in the leishmaniae.
作者信息
Simon M W, Martin E, Mukkada A J
出版信息
J Bacteriol. 1978 Sep;135(3):895-9. doi: 10.1128/jb.135.3.895-899.1978.
Abstract
Isocitrate lyase (EC 4.1.3.1) and malate synthase (EC 4.1.3.2), the two enzymes characteristic of the glyoxylate cycle, were demonstrated in promastigotes of five species of Leishmania (L. brasiliensis, L. donovani, L. mexicana, L. tarentolae, and L. tropica). Both enzymes were present in cells grown in a medium containing 10 mM glucose. Substitution of glucose with 20 mM acetate did not enhance enzyme levels. Acetate was readily taken up and metabolized by the cells. The distribution of label from acetate into various intermediary metabolites indicates a functional glyoxylate cycle and its role in gluconeogenesis/glyconeogenesis. The glyoxylate cycle in conjunction with alanine-glyoxylate aminotransferase and glyoxylate-aspartate aminotransferase could also be important in providing glyoxylate, the precursor for glycine biosynthesis.
摘要
异柠檬酸裂解酶（EC 4.1.3.1）和苹果酸合酶（EC 4.1.3.2）是乙醛酸循环的两种特征性酶，在五种利什曼原虫（巴西利什曼原虫、杜氏利什曼原虫、墨西哥利什曼原虫、热带利什曼原虫和碲利什曼原虫）的前鞭毛体中得到了证实。这两种酶都存在于在含有10 mM葡萄糖的培养基中生长的细胞中。用20 mM乙酸盐替代葡萄糖并没有提高酶的水平。乙酸盐很容易被细胞摄取并代谢。乙酸盐中的标记物在各种中间代谢产物中的分布表明存在功能性乙醛酸循环及其在糖异生/糖原异生中的作用。乙醛酸循环与丙氨酸-乙醛酸转氨酶和乙醛酸-天冬氨酸转氨酶一起，在提供甘氨酸生物合成的前体乙醛酸方面也可能很重要。
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