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Literature summary extracted from

  • de Queiroz, M.S.; Waldrop, G.L.
    Modeling and numerical simulation of biotin carboxylase kinetics: implications for half-sites reactivity (2007), J. Theor. Biol., 246, 167-175.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.14 Escherichia coli
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.14 ATP + biotin-carboxyl-carrier protein + CO2 mathematical modeling and numerical simulations of the kinetics of wild-type, hybrid dimers, and mutant homodimers of biotin carboxylase are performed. Numerical simulations of biotin carboxylase kinetics are the most similar to the experimental data when an oscillating active site model is used. In contrast, alternative models where the active sites are independent do not agree with the experimental data. Thus, the numerical simulations of the proposed kinetic model support the hypothesis that the two active sites of biotin carboxylase alternate their catalytic cycles Escherichia coli ADP + phosphate + carboxybiotin-carboxyl-carrier protein
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