ArticleApplied and environmental microbiology2009
Molecular determinants of the regioselectivity of toluene/o-xylene monooxygenase from Pseudomonas sp. strain OX1.
Article in Applied and environmental microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 33 citations in OpenAlex.
- Drug Metabolism by Engineered Toluene o-Xylene Monooxygenases of Pseudomonas sp. OX1.Biotechnology and bioengineering · 2026Article
- Molecular Dissection of dH3w, A Fluorescent Peptidyl Sensor for Zinc and Mercury.Sensors (Basel, Switzerland) · 2020Article
- Denatured lysozyme-coated carbon nanotubes: a versatile biohybrid material.Scientific reports · 2019Article
- The Toluene o-Xylene Monooxygenase Enzymatic Activity for the Biosynthesis of Aromatic Antioxidants.PloS one · 2015Article
- Gates of enzymes.Chemical reviews · 2013Review
- Engineering non-heme mono- and dioxygenases for biocatalysis.Computational and structural biotechnology journal · 2012Review
- Tuning the specificity of the recombinant multicomponent toluene o-xylene monooxygenase from Pseudomonas sp. strain OX1 for the biosynthesis of tyrosol from 2-phenylethanol.Applied and environmental microbiology · 2011Article
- Insights into the different dioxygen activation pathways of methane and toluene monooxygenase hydroxylases.Journal of the American Chemical Society · 2011Article
- Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex.The Journal of biological chemistry · 2011Article
- Crystallization and preliminary X-ray analysis of PaaAC, the main component of the hydroxylase of the Escherichia coli phenylacetyl-coenzyme A oxygenase complex.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial multicomponent monooxygenases (BMMs) are a heterogeneous family of di-iron monooxygenases which share the very interesting ability to hydroxylate aliphatic and/or aromatic hydrocarbons. Each BMM possesses defined substrate specificity and regioselectivity which match the metabolic requirements of the strain from which it has been isolated. Pseudomonas sp. strain OX1, a strain able to metabolize o-, m-, and p-cresols, produces the BMM toluene/o-xylene monooxygenase (ToMO), which converts toluene to a mixture of o-, m-, and p-cresol isomers. In order to investigate the molecular determinants of ToMO regioselectivity, we prepared and characterized 15 single-mutant and 3 double-mutant forms of the ToMO active site pocket. Using the Monte Carlo approach, we prepared models of ToMO-substrate and ToMO-reaction intermediate complexes which allowed us to provide a molecular explanation for the regioselectivities of wild-type and mutant ToMO enzymes. Furthermore, using binding energy values calculated by energy analyses of the complexes and a simple mathematical model of the hydroxylation reaction, we were able to predict quantitatively the regioselectivities of the majority of the variant proteins with good accuracy. The results show not only that the fine-tuning of ToMO regioselectivity can be achieved through a careful alteration of the shape of the active site but also that the effects of the mutations on regioselectivity can be quantitatively predicted a priori.
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