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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Amino acids 6 (1994), S. 261-272 
    ISSN: 1438-2199
    Keywords: Amino acids ; Flux control ; Flux quantification ; Lysine production ; Gene exchange ; Metabolic design ; Amino acid export
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The Gram positive bacteriumCorynebacterium glutamicum is used for the production of L-lysine. This review focuses on the progress achieved in the past five years for a deeper understanding of lysine overproduction. This period also coincides with decisive progress in the use of genetic engineering techniques for analysing and increasing the metabolite flux inC. glutamicum. It was thus demonstrated that thein vivo activity of the allosterically controlled aspartate kinase is important for flux control, but in addition also the amount of the dihydrodipicolinate synthase. An outstanding feature ofC. glutamicum is the split lysine biosynthesis pathway. NMR investigations have clearly shown that both pathways are simultaneously usedin vivo and that the flux ratio depends on nitrogen availability. The cellular synthesized lysine is eventually exported into the external medium through a specific carrier. Interestingly lysine producers have other export characteristics so that the carrier properties also seem to be important for increased metabolite flux.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-072X
    Keywords: Induction ; Carbon catabolite repression ; Alcohol oxidase ; Catalase ; Methanol ; Mixed substrates ; Continuous culture ; Hansenula polymorpha
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The regulation of the synthesis of alcohol oxidase, catalase, formaldehyde dehydrogenase and formate dehydrogenase was investigated in the methanol-utilizing yeast Hansenula polymorpha. The organism was found to synthesize immunologically identical alcohol oxidases during growth on glycerol and methanol. Growth on glycerol, however, was not dependent on the alcohol oxidase, as was shown with a mutant without alcohol oxidase protein. Similarly it was shown with a catalase activity negative mutant that high catalase activity during growth on glycerol was not a prerequisite for the utilization of this substrate, though absolutely required for growth on methanol. Experiments were conducted with mixed substrates to study the influence of methanol on alcohol oxidase synthesis. In batch cultures, growth on ribose plus methanol resulted in an enhanced rate of alcohol oxidase synthesis as compared to ribose alone. In continuous cultures, (D=0.1 h-1) addition of methanol to glycerol-, glucose-, or sorbose-limited cultures gave rise to increased alcohol oxidase activity of up to 20 U/mg, which is about by 2 times higher than the specific activity used for growth on methanol alone. The increase in specific activity of the dissimilatory enzymes on the mixed substrates is partly due to methanol per se, as was shown by a mutant unable to dissimilate or assimilate methanol.
    Type of Medium: Electronic Resource
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