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Deputy Director of National Reference Center
Deputy Head of Facility
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Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region

NMR, CD and IR spectroscopies of a tridecanucleotide containing a no-base residue: coexistence of B and Z conformations

© Research

Publication : The Journal of biological chemistry

Nucleotide sequence of lysC gene encoding the lysine-sensitive aspartokinase III of Escherichia coli K12. Evolutionary pathway leading to three isofunctional enzymes

Team: Archived: Molecular Microbial Pathogenesis

Member: Claude Parsot

Scientific Fields

Diseases

Organisms

Applications

Technique

Published in The Journal of biological chemistry - 25 Jan 1986

Cassan M, Parsot C, Cohen GN, Patte JC

Link to Pubmed [PMID] – 3003049

J. Biol. Chem. 1986 Jan;261(3):1052-7

The lysC gene encoding the lysine-sensitive aspartokinase III of Escherichia coli K12 has been cloned and its nucleotide sequence determined. Analysis of the deduced protein sequence (449 amino acid residues) reveals that the entire sequence of aspartokinase III is homologous to the N-terminal part of the two iso- and bifunctional aspartokinase-homoserine dehydrogenases I and II of E. coli. An evolutionary pathway leading to the three molecular species present in the same organism is proposed, and the possible involvement of a highly conserved region in subunit interactions is discussed.

Published on: 25 Jan 1986