The theoretical analysis of kinetic behaviour of “hysteretic” allosteric enzymes. I. The kinetic manifestations of slow conformational change of an oligomeric enyzme in the Monod, Wyman and Changeux model

Bi, Kurganov; Dorozhko, A.I.; Kagan, Z. S.; Yakovlev, V.A.

doi:10.1016/0022-5193(76)90059-x

Cited by 46 publications

(26 citation statements)

References 44 publications

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“…Furthermore, the Kurganov's et al (26) theoretical study predicts dependencies of on [S] 0 similar to those ones obtained experimentally for PPO (Fig. 2C) along with curves of product accumulation similar to those ones observed experimentally (Fig.…”

Section: Hysteresis and Cooperativitysupporting

confidence: 84%

Hysteresis and Positive Cooperativity of Iceberg Lettuce Polyphenol Oxidase

Chazarra

García‐Carmona

Cabanes

2001

Biochemical and Biophysical Research Communications

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Section: Hysteresis and Cooperativitysupporting

confidence: 84%

Hysteresis and Positive Cooperativity of Iceberg Lettuce Polyphenol Oxidase

Chazarra

García‐Carmona

Cabanes

2001

Biochemical and Biophysical Research Communications

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“…Obviously, this time lag is caused by the comparatively slow change of the enzyme from an unassociated, less active (inactive) state to an associated state of high(er) activity. According to Kurganov [17,18], the formation of product (P) by self-associating systems can be described by …”

Section: Resultsmentioning

confidence: 99%

myo‐Inositol oxygenase from rat kidneys

Koller¹,

Koller²

1990

European Journal of Biochemistry

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“…In previous studies at 30°C, the maximum capacity of PFK estimated in cell extracts was close to the in vivo flux through this enzyme (48). The difference between these parameters in cultures grown at 12°C may reflect suboptimal conditions in the enzyme assays due to temperature-dependent changes in the complex allosteric regulation of this enzyme (49,50). A deeper understanding of the in vivo kinetics of glycolysis at low temperature, involving the application of kinetic modeling, will require quantitative data on the impact of temperature on the kinetics and allosteric regulation of the entire glycolytic pathway in S. cerevisiae.…”

Section: Tablementioning

confidence: 99%

Control of the Glycolytic Flux in Saccharomyces cerevisiae Grown at Low Temperature

Tai

Daran‐Lapujade

Luttik

et al. 2007

Journal of Biological Chemistry

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Growth temperature has a profound impact on the kinetic properties of enzymes in microbial metabolic networks. Activities of glycolytic enzymes in Saccharomyces cerevisiae were up to 7.5-fold lower when assayed at 12°C than at 30°C. Nevertheless, the in vivo glycolytic flux in chemostat cultures (dilution rate: 0.03 h ؊1 ) grown at these two temperatures was essentially the same. To investigate how yeast maintained a constant glycolytic flux despite the kinetic challenge imposed by a lower growth temperature, a systems approach was applied that involved metabolic flux analysis, transcript analysis, enzyme activity assays, and metabolite analysis. Expression of hexosetransporter genes was affected by the growth temperature, as indicated by differential transcription of five HXT genes and changed zero trans-influx kinetics of [ 14 C]glucose transport. No such significant changes in gene expression were observed for any of the glycolytic enzymes. Fermentative capacity (assayed off-line at 30°C), which was 2-fold higher in cells grown at 12°C, was therefore probably controlled predominantly by glucose transport. Massive differences in the intracellular concentrations of nucleotides (resulting in an increased adenylate energy charge at low temperature) and glycolytic intermediates indicated a dominant role of metabolic control as opposed to gene expression in the adaptation of glycolytic enzyme activity to different temperatures. In evolutionary terms, this predominant reliance on metabolic control of a central pathway, which represents a significant fraction of the cellular protein of the organism, may be advantageous to limit the need for protein synthesis and degradation during adaptation to diurnal temperature cycles.Changing ambient temperature, for example, as a result of diurnal temperature cycling, is among the most common environmental changes that microorganisms have to contend with in nature. Temperature effects on microbial physiology are also relevant for the industrial exploitation of microorganisms. For example, the temperature in industrial processes for production of alcoholic beverages with the yeast Saccharomyces cerevisiae (commonly 8 -20°C) is much lower than the optimum temperature range for growth (25-30°C) (1).Much of the current knowledge on adaptation of the model eukaryote S. cerevisiae to suboptimal temperatures has been derived from studies on cold shock. These studies have identified cold-induced changes in membrane lipid composition (2), transport functions, translational efficiency, protein folding, and nucleic acid structure (for a review, see Ref.3). Transcriptome analysis of cold adaptation in S. cerevisiae has revealed several types of responses that depend on the temperature range applied, namely "cold shock" (between 20 and 10°C) (4, 5) and "near freezing" (Ͻ10°C) (6) conditions. Responses to low temperature are also affected by the exposure period to low temperature (early phase and late phase responses (4, 6)). The early response in cold shock experiments encompasses upregulati...

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The theoretical analysis of kinetic behaviour of “hysteretic” allosteric enzymes. I. The kinetic manifestations of slow conformational change of an oligomeric enyzme in the Monod, Wyman and Changeux model

Cited by 46 publications

References 44 publications

Hysteresis and Positive Cooperativity of Iceberg Lettuce Polyphenol Oxidase

Hysteresis and Positive Cooperativity of Iceberg Lettuce Polyphenol Oxidase

myo‐Inositol oxygenase from rat kidneys

Control of the Glycolytic Flux in Saccharomyces cerevisiae Grown at Low Temperature

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