Quantitative analysis of the fermentative metabolism

Savitsky1,3 1Department of Chemistry, M. Lomonosov Moscow State University 2N. The chromophore group based on the hydroxybenzylidene-imidazoline molecule, which is formed in nature from three amino-acid residues inside the protein globule and well shielded from external media, is responsible for light absorption and fluorescence. Along with the intense experimental studies of the properties of fluorescent proteins and their chromophores by biochemical, X-ray, and spectroscopic tools, in recent years, computer modeling has been used to characterize their properties and spectra.

Quantitative analysis of the fermentative metabolism

Abstract A major challenge in systems biology lies in the integration of processes occurring at different levels, such as transcription, translation, and metabolism, to understand the functioning of a living cell in its environment.

We studied the high temperature-induced glycolytic flux increase in Saccharomyces cerevisiae and investigated the regulatory mechanisms underlying this increase. We used glucose-limited chemostat cultures to separate regulatory effects of temperature from effects on growth rate.

Quantitative analysis of the fermentative metabolism

We observed an increased flux through all enzymes, ranging from 5- to fold. We quantified the contributions of direct temperature effects on enzyme activities, the gene expression cascade and shifts in the metabolic network, to the increased flux through each enzyme.

To do this we adapted flux regulation analysis. We show that the direct effect of temperature on enzyme kinetics can be included as a separate term.

Quantitative analysis of the fermentative metabolism

Together with hierarchical regulation and metabolic regulation, this term explains the total flux change between two steady states. Surprisingly, the effect of the cultivation temperature on enzyme catalytic capacity, both directly through the Arrhenius effect and indirectly through adapted gene expression, is only a moderate contribution to the increased glycolytic flux for most enzymes.

The changes in flux are therefore largely caused by changes in the interaction of the enzymes with substrates, products, and effectors. The costs of publication of this article were defrayed in part by the payment of page charges.

Section solely to indicate this fact. Received April 15, Revision received May 27, Between and , the Nobel Prizes and the Prize in Economic Sciences were awarded times to people and organizations.

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