Sequence of the Escherichia coli fructose-1,6-bisphosphatase gene.
Sequence of the Escherichia coli fructose-1,6-bisphosphatase gene.
复制标题
大肠杆菌果糖-1,6-双磷酸酶基因的序列。
作者：
W. D. Hamilton;D. Harrison;T. Dyer
果糖-1，6-二磷酸酶(FBPase)是一种存在于多种生物体中的酶。虽然它们的催化功能基本相同，但它的确切作用并不相同，因为它可能是几种不同代谢途径的组成部分。例如，在大肠杆菌中，它是在琥珀酸甘油和醋酸酯等物质上生长所必需的。我们已经对该蛋白(1，2)的大肠杆菌基因进行了测序，以便我们可以将预测的其产物的氨基酸序列与其他已知的FBPase序列进行比较。叶绿体(3)、哺乳动物(4，5)、酵母(6)和大肠杆菌FBPase中保守的氨基酸用(*)标记。推测的编码序列包含332个密码子，给出了一个预测分子量为36,834的蛋白质。由于几个区域的氨基酸在所有研究的FBPase中都是保守的，似乎所有的基因都有一个共同的祖先。然而，正如其他地方(3)所讨论的那样，祖先序列已经进化，因此酶的活性可以被调节以适应它必须在其中发挥作用的特定的亚细胞环境。
Fructose-1,6-bisphosphatase (FBPase) is an enzyme found in many different types of organism. Although it has basically the same catalytic function in each, its precise role is not the same as it may be a component of several different metabolic pathways. In E. coli, for example, it is necessary for growth on substances such as glycerol succinate and acetate. We have sequenced the E. coli gene for this protein (1,2) so that we could compare the predicted amino acid sequence of its product with other known FBPase sequences. Amino acids conserved in chloroplasts (3) mammals (4,5), yeasts (6), and E. coli FBPases are marked with (*). The putative coding sequence contains 332 codons giving a protein of predicted molecular weight 36,834. As amino acids in several regions are conserved in all the FBPases studied, it would seem probable that all the genes had a common progenitor. However, as discussed elsewhere (3), the ancestral sequence has evolved so that the activity of the enzyme can be regulated to suit the particular subcellular environment in which it must function.