This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Thèze, J. Articles by Patte, J. C. Search for Related Content PubMed PubMed Citation Articles by Thèze, J. Articles by Patte, J. C.

Mapping of the Structural Genes of the Three Aspartokinases and of the Two Homoserine Dehydrogenases of Escherichia coli K-12

¹ Service de Biochimie Cellulaire, Institut Pasteur, 75015 Paris, France and Institut de Microbiologie, Faculté des Sciences, Université Paris XI, 91405 Orsay, France

ABSTRACT

Mutants requiring threonine plus methionine (or homoserine), or threonine plus methionine plus diaminopimelate (or homoserine plus diaminopimelate) have been isolated from strains possessing only one of the three isofunctional aspartokinases. They have been classified in several groups according to their enzymatic defects. Their mapping is described. Several regions of the chromosome are concerned: thrA (aspartokinase I-homoserine dehydrogenase I) is mapped in the same region as thrB and thrC (0 min). lysC (aspartokinase III) is mapped at 80 min, far from the other genes coding for diaminopimelate synthesis. metLM (aspartokinase II-homoserine dehydrogenase II) lies at 78 min closely linked to metB, metJ, and metF.

This article has been cited by other articles:

• Cahyanto, M. N., Kawasaki, H., Nagashio, M., Fujiyama, K., Seki, T. (2006). Regulation of aspartokinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase in Lactobacillus plantarum. Microbiology 152: 105-112 [Abstract] [Full Text]  
• Hardie, K. R., Cooksley, C., Green, A. D., Winzer, K. (2003). Autoinducer 2 activity in Escherichia coli culture supernatants can be actively reduced despite maintenance of an active synthase, LuxS. Microbiology 149: 715-728 [Abstract] [Full Text]  
• Hernando-Rico, V., Martin, J. F., Santamarta, I., Liras, P. (2001). Structure of the ask-asd operon and formation of aspartokinase subunits in the cephamycin producer 'Amycolatopsis lactamdurans'. Microbiology 147: 1547-1555 [Abstract] [Full Text]  
• Val, D. L., Cronan, J. E. Jr. (1998). In Vivo Evidence that S-Adenosylmethionine and Fatty Acid Synthesis Intermediates Are the Substrates for the LuxI Family of Autoinducer Synthases. J. Bacteriol. 180: 2644-2651 [Abstract] [Full Text]  
• King, N. D., O'Brian, M. R. (2001). Evidence for Direct Interaction between Enzyme INtr and Aspartokinase to Regulate Bacterial Oligopeptide Transport. J. Biol. Chem. 276: 21311-21316 [Abstract] [Full Text]