Amino acid sequence homology among fructose-1,6-bisphosphatases.
Amino acid sequence homology among fructose-1,6-bisphosphatases.
复制标题
DOI：
10.1016/0006-291x(86)90005-7
复制
发表时间：
1986-03
影响因子：
3.1
通讯作者：
F. Marcus;B. Gontero;P. Harrsch;J. Rittenhouse
中科院分区：
文献类型：
--
作者：
F. Marcus;B. Gontero;P. Harrsch;J. Rittenhouse
果糖1,6 -二磷酸水解为果糖6-磷酸是碳水化合物代谢的关键反应。催化这一反应的酶，果糖- 1,6 -二磷酸酶，似乎存在于所有形式的生物体中。然而，酶活性的调节是通过多种不同的机制发生的。这些包括AMP抑制（大多数来源），环AMP依赖性磷酸化（酵母）和光依赖性激活（叶绿体）。在本研究中，我们将哺乳动物果糖- 1,6 -双磷酸酶的初级结构与从酵母、酿酒酵母、大肠杆菌和菠菜叶绿体酶中分离的肽序列进行了比较。我们的研究结果显示了高度的序列同源性，表明所有果糖- 1,6 -双磷酸酶具有共同的进化起源。
Abstract The hydrolysis of fructose 1, 6-bisphosphate to fructose 6-phosphate is a key reaction of carbohydrate metabolism. The enzyme that catalyzes this reaction, fructose-1, 6-bisphosphatase, appears to be present in all forms of living organisms. Regulation of the enzyme activity, however, occurs by a variety of distinct mechanisms. These include AMP inhibition (most sources), cyclic AMP-dependent phosphorylation (yeast), and light-dependent activation (chloroplast). In the present studies, we have made a comparison of the primary structure of mammalian fructose-1, 6-bisphosphatase with the sequence of peptides isolated from the yeast Saccharomyces cerevisiae, Escherichia coli, and spinach chloroplast enzymes. Our results demonstrate a high degree of sequence homology, suggesting a common evolutionary origin for all fructose-1, 6-bisphosphatases.