Abstract

Benzoate Concentration and Cooperativity by a Substrate for Benzoate 1,2-dioxygenase from Benzoate-Degrading Rhodococcus Opacus 1CP

Highlights

  • Introduction concentrationA sigmoidal but not Michaelis-MentenUnder aerobic conditions the initial attack of hyperbolic plot of the dependency of the rate of different substrates by bacteria is usually performed by enzymatic reaction on the initial substrate concentration mono- or dioxygenases [1]

  • Benzoate degradation under aerobic conditions starts from an initial attack of this compound by benzoate 1,2-dioxygenase (BDO)

  • We have shown that the change of freshly harvested cells respiration in the presence of benzoate was an indicator of BDO activity of R.opacus 1CP cells [8]

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Summary

Introduction

Under aerobic conditions the initial attack of hyperbolic plot of the dependency of the rate of different substrates by bacteria is usually performed by enzymatic reaction on the initial substrate concentration mono- or dioxygenases [1]. In many cases these is typical for allosteric enzymes. The BDO activity in a cell-free extract could not always be determined even if the depletion of substrate was registered [6]. The rate of BDO reaction is determined in whole cells by monitoring their respiration in the presence of respiration substrate [7]. While studying growth of R. opacus 1CP on benzoate as a sole source of carbon we found that growth characteristics of the culture and a kinetics of enzymatic reactions and the enzyme pool of the cell were changing when the

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