Internal homologies in the two aspartokinase-homoserine dehydrogenases of Escherichia coli K-12.

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.

authors

Ferrara P,Duchange N,Zakin MM,Cohen GN

doi

10.1073/pnas.81.10.3019

subject

Has Abstract

pub_date

1984-05-01 00:00:00

pages

3019-23

issue

10

eissn

0027-8424

issn

1091-6490

journal_volume

81

pub_type

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