大肠杆菌K-12中两种天冬氨酸激酶-高丝氨酸脱氢酶的内部同源性。
Internal homologies in the two aspartokinase-homoserine dehydrogenases of Escherichia coli K-12.
作者信息
Ferrara P, Duchange N, Zakin M M, Cohen G N
出版信息
Proc Natl Acad Sci U S A. 1984 May;81(10):3019-23. doi: 10.1073/pnas.81.10.3019.
Abstract
In Escherichia coli, AK I- HDH I and AK II- HDH II are two bifunctional proteins, derived from a common ancestor, that catalyze the first and third reactions of the common pathway leading to threonine and methionine. An extensive amino acid sequence comparison of both molecules reveals two main features on each of them: (i) two segments, each of about 130 amino acids, covering the first one-third of the polypeptide chain, are similar to each other and (ii) two segments, each of about 250 amino acids and covering the COOH-terminal 500 amino acids also present a significant homology. These findings suggest that these two regions may have evolved independently of each other by a process of gene duplication and fusion previous to the appearance of an ancestral aspartokinase-homoserine dehydrogenase molecule.
摘要
在大肠杆菌中，AK I - HDH I和AK II - HDH II是两种双功能蛋白，它们源自一个共同的祖先，催化通向苏氨酸和蛋氨酸的共同途径的第一步和第三步反应。对这两种分子进行广泛的氨基酸序列比较，发现它们各自有两个主要特征：（i）两个片段，每个片段约130个氨基酸，覆盖多肽链的前三分之一，彼此相似；（ii）两个片段，每个片段约250个氨基酸，覆盖COOH末端的500个氨基酸，也存在显著的同源性。这些发现表明，这两个区域可能在祖先天冬氨酸激酶 - 高丝氨酸脱氢酶分子出现之前，通过基因复制和融合过程彼此独立进化。
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