E.coli aspartokinase II-homoserine dehydrogenase II polypeptide chain has a triglobular structure

Belfaiza, J; Fazel, Akram M.; Müller, K; Cohen, Georges N.

doi:10.1016/0006-291x(84)90373-5

Cited by 10 publications

(1 citation statement)

References 11 publications

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“…Accordingly, for control coefficients for large changes, the multiplier r PTS is deduced in an independent manner-from that used in Equation (3)-through increasing the total IICB Glc by a factor of 1.14. b The bifunctional enzyme aspartate kinase I-homoserine dehydrogenase I in our kinetic model is responsible for less than 10% of the flux through total AK activity but all the HDH activity. It should be noted that each of these activities resides on separate structural domains (Belfaiza et al, 1984;Chassagnole et al, 2001a).…”

Section: Discussionmentioning

confidence: 99%

In silico strategy to rationally engineer metabolite production: A case study for threonine in Escherichia coli

Rodríguez-Prados

Atauri

Maury

et al. 2009

Biotech & Bioengineering

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Genetic engineering of metabolic pathways is a standard strategy to increase the production of metabolites of economic interest. However, such flux increases could very likely lead to undesirable changes in metabolite concentrations, producing deleterious perturbations on other cellular processes. These negative effects could be avoided by implementing a balanced increase of enzyme concentrations according to the Universal Method [Kacser and Acerenza (1993) Eur J Biochem 216:361-367]. Exact application of the method usually requires modification of many reactions, which is difficult to achieve in practice. Here, improvement of threonine production via pyruvate kinase deletion in Escherichia coli is used as a case study to demonstrate a partial application of the Universal Method, which includes performing sensitivity analysis. Our analysis predicts that manipulating a few reactions is sufficient to obtain an important increase in threonine production without major perturbations of metabolite concentrations.

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Section: Discussionmentioning

confidence: 99%

In silico strategy to rationally engineer metabolite production: A case study for threonine in Escherichia coli

Rodríguez-Prados

Atauri

Maury

et al. 2009

Biotech & Bioengineering

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Regulation of Amino Acids Biosynthesis in Prokaryotes

Cohen

1987

Signal Transduction and Protein Phosphorylation

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Evolutionary relationships between yeast and bacterial homoserine dehydrogenases

1993

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The Saccharomyces cerevisiae HOM6 gene, encoding homoserine dehydrogenase (EC 1.1.1.3) was cloned and its nucleotide sequence determined. The yeast homoserine dehydrogenase shows extensive homology to the homoserine dehydrogenase domains of the two aspartokinase‐homoserine dehydrogenases from Escherichia coli as well as to the homoserine dehydrogenases from Gram positive bacteria. Sequence alignment reveals that the yeast enzyme is the smallest homoserine dehydrogenase known, owing to the absence of a C‐terminal domain endowed with the l‐threonine allosteric response in Gram positive bacteria. Accordingly, the S. cerevisiae enzyme appears to be a naturally occurring feedback resistant homoserine dehydrogenase. Our results indicate that homoserine dehydrogenase was originally an unregulated enzyme and that feedback control acquisition occured twice during evolution after the divergence between Gram positive and Gram negative bacteria.

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E.coli aspartokinase II-homoserine dehydrogenase II polypeptide chain has a triglobular structure

Cited by 10 publications

References 11 publications

In silico strategy to rationally engineer metabolite production: A case study for threonine in Escherichia coli

In silico strategy to rationally engineer metabolite production: A case study for threonine in Escherichia coli

Regulation of Amino Acids Biosynthesis in Prokaryotes

Evolutionary relationships between yeast and bacterial homoserine dehydrogenases

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