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Biology 2015, 4(2), 424-442;

Structural Organization of Enzymes of the Phenylacetate Catabolic Hybrid Pathway

Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E5, Canada
Author to whom correspondence should be addressed.
Academic Editor: Thorsten Berg
Received: 10 March 2015 / Revised: 25 May 2015 / Accepted: 29 May 2015 / Published: 12 June 2015
(This article belongs to the Special Issue Protein-Protein Interactions)
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Aromatic compounds are the second most abundant class of molecules on the earth and frequent environmental pollutants. They are difficult to metabolize due to an inert chemical structure, and of all living organisms, only microbes have evolved biochemical pathways that can open an aromatic ring and catabolize thus formed organic molecules. In bacterial genomes, the phenylacetate (PA) utilization pathway is abundant and represents the central route for degradation of a variety of organic compounds, whose degradation reactions converge at this pathway. The PA pathway is a hybrid pathway and combines the dual features of aerobic metabolism, i.e., usage of both oxygen to open the aromatic ring and of anaerobic metabolism—coenzyme A derivatization of PA. This allows the degradation process to be adapted to fluctuating oxygen conditions. In this review we focus on the structural and functional aspects of enzymes and their complexes involved in the PA degradation by the catabolic hybrid pathway. We discuss the ability of the central PaaABCE monooxygenase to reversibly oxygenate PA, the controlling mechanisms of epoxide concentration by the pathway enzymes, and the similarity of the PA utilization pathway to the benzoate utilization Box pathway and β-oxidation of fatty acids. View Full-Text
Keywords: phenylacetate degradation; catabolic pathway; paa operon; three-dimensional structure phenylacetate degradation; catabolic pathway; paa operon; three-dimensional structure

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Grishin, A.M.; Cygler, M. Structural Organization of Enzymes of the Phenylacetate Catabolic Hybrid Pathway. Biology 2015, 4, 424-442.

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