Literature DB >> 2200929

Cellular concentrations of enzymes and their substrates.

K R Albe1, M H Butler, B E Wright.   

Abstract

The activity of crude and pure enzyme preparations as well as the molecular weight of these enzymes were obtained from the literature for several organisms. From these data enzyme concentrations were calculated and compared to the concentration(s) of their substrates in the same organism. The data are expressed as molar ratios of metabolite concentration to enzyme site concentration. Of the 140 ratios calculated, 88% were one or greater, indicating that in general substrates exceed their cognate enzyme concentrations. Of the 17 cases where enzyme exceeds metabolite concentration, 16 were in glycolysis. The data in general justify the use of enzyme kinetic mechanisms determined in vitro in the construction of dynamic models which simulate in vivo metabolism.

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Year:  1990        PMID: 2200929     DOI: 10.1016/s0022-5193(05)80266-8

Source DB:  PubMed          Journal:  J Theor Biol        ISSN: 0022-5193            Impact factor:   2.691


  102 in total

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2.  Kinetics of the monomer-dimer reaction of yeast hexokinase PI.

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4.  Evolution of dominance in metabolic pathways.

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5.  Design and use of fluorescent fusion proteins in cell biology.

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6.  Minimization of intermediate concentrations as a suggested optimality principle for biochemical networks. II. Time hierarchy, enzymatic rate laws, and erythrocyte metabolism.

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7.  Introducing total substrates simplifies theoretical analysis at non-negligible enzyme concentrations: pseudo first-order kinetics and the loss of zero-order ultrasensitivity.

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Journal:  J Math Biol       Date:  2009-03-31       Impact factor: 2.259

8.  In silico Geobacter sulfurreducens metabolism and its representation in reactive transport models.

Authors:  E L King; K Tuncay; P Ortoleva; C Meile
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9.  A high-throughput SAMDI-mass spectrometry assay for isocitrate dehydrogenase 1.

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Review 10.  Oxidative protein folding: from thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum.

Authors:  Devin A Hudson; Shawn A Gannon; Colin Thorpe
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