Regiospecificity of two multicomponent monooxygenases from Pseudomonas stutzeri OX1: Molecular basis for catabolic adaptation of this microorganism to methylated aromatic compounds

Article Abstract:

The kinetics and regioselectivity of toluene and o-xylene oxidation is investigated using Escherichia coli cells expressing toluene o-xylene monooxygenase (ToMO) and phenol hydroxylase (PH) complexes. It is found that using the two enzymes in a concerted way confers on the strain a selective advantage based on the ability of the microorganism to optimize the efficiency of the use of nohydroxylated aromatic hydrocarbons.

Genetic aspects, Biodegradation, Oxidation-reduction reaction, Oxidation-reduction reactions

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Phenol hydroxylase and toulene/o-xylene monooxygenase from Pseudomonas stutzeri OX1: interplay between two enzymes

Article Abstract:

The new phenol hydroxylase (PH) from Pseudomonas is examined and characterized for understanding the metabolic significance of the association of PH and toulene/o-xylene monooxygenase (ToMO), which display similar enzymatic activities in the same microorganisms. The use of benzene in Pseudomonas stutzeri OX1 can be optimized using ToMO and PH.

Science & research, Cyclic crudes and intermediates, Cyclic Crude and Intermediate Manufacturing, Phenol, Research, Metabolism, Phenol (Compound)

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Mutation of glutamic acid 103 of toluene o-xylene monooygenase as a means to control the catabolic efficiency of a recombinant upper pathway for degradation of methylated aromatic compounds

Article Abstract:

The possibility of producing toluene o-xylene monooxygenase (ToMO) mutants with modified regioselectivity are compared with the regioselectivity of the wild type protein. It indicates that rational design of ToMO mutants with altered regioselectivity are used to tune the relative abundance of the products of toluene and o-xylene hydroxylation.

Glutamate, Hydroxylation, Properties

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