By L. Eggeling, H. Sahm, A. A. de Graaf (auth.), H. Sahm, C. Wandrey (eds.)
Contents:L. Eggeling, H. Sahm, A.A. de Graaf: Quantifying and Directing Metabolite Flux: program to Amino Acid Overproduction.-
R. Krämer: research and Modeling of Substrate Uptake and Product free up by way of Prokaryotic and Eukaryotic Cells.-
D. Weuster-Botz, A.A. de Graaf: response Engineering the way to learn Intracellular Metabolite Concentrations.-
W. Wiechert, A.A. de Graaf: In Vivo desk bound Flux research via 13C Labeling Experiments.-
B. Sonnleitner: New techniques for Quantitative Bioprocess study and Development.
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Ishino S, Shimomura-Nishimuta J, Yamaguchi K, Shirahata K, Araki K (1991) J Gen Appl Microbiol Tokyo 37:157 102. Shaffstein ST, Tucker SN, Mancuso A, Blanch HW, Clark DS (1994) Biotech Bioeng 43:1059 103. Schrumpf B, Eggeling L, Sahm H (1992) Appl Microbiol Biotechnol 37:566 104. Oguiza JA, Malumbres M, Erian G, Pisabarro A, Mateos LM, Martin F, Martin JF (1993) J Bacteriol 175:7356 105. Schrumpf B (1991) Diss. Universit/it Disseldorf 106. Cremer J, Treptow C, Eggeling L, Sahm H (1988) J Gen Microbiol 134:3221 107.
At elevated flux and metabolite concentrations, however, many previously unimportant mechanisms might come into play, requiring strategies to be pursued to reach targets completely different from the original target of the strain construction. Thus, for instance, (iv) degrading activities of competing pathways might become relevant, requiring the inactivation of corresponding enzymes [115], (v) osmotic effects might occur [ 116-118], (vi) the tolerance towards intermediates might be reduced [22, 119], or (vii) excretion activities might become limiting [105].
The second reaction of relevance for flux increase is dihydrodipicolinate synthase. Although, according to general features of flux control this branch point enzyme was a candidate for lysine flux increase, its importance has not been recognized until recently. This is probably due to the fact that biochemical analysis has shown that the enzyme is neither allosterically controlled nor repressed [106]. The synthase competes with the homoserine dehydrogenase for the common substrate aspartate semialdehyde and is controlled in its activity [135] and synthesis as well [136, 137].
