Biodegradation of Aromatic Compounds by Escherichia coli
Open Access
- 1 December 2001
- journal article
- review article
- Published by American Society for Microbiology in Microbiology and Molecular Biology Reviews
- Vol. 65 (4), 523-569
- https://doi.org/10.1128/mmbr.65.4.523-569.2001
Abstract
Although Escherichia coli has long been recognized as the best-understood living organism, little was known about its abilities to use aromatic compounds as sole carbon and energy sources. This review gives an extensive overview of the current knowledge of the catabolism of aromatic compounds by E. coli. After giving a general overview of the aromatic compounds that E. coli strains encounter and mineralize in the different habitats that they colonize, we provide an up-to-date status report on the genes and proteins involved in the catabolism of such compounds, namely, several aromatic acids (phenylacetic acid, 3- and 4-hydroxyphenylacetic acid, phenylpropionic acid, 3-hydroxyphenylpropionic acid, and 3-hydroxycinnamic acid) and amines (phenylethylamine, tyramine, and dopamine). Other enzymatic activities acting on aromatic compounds in E. coli are also reviewed and evaluated. The review also reflects the present impact of genomic research and how the analysis of the whole E. coli genome reveals novel aromatic catabolic functions. Moreover, evolutionary considerations derived from sequence comparisons between the aromatic catabolic clusters of E. coli and homologous clusters from an increasing number of bacteria are also discussed. The recent progress in the understanding of the fundamentals that govern the degradation of aromatic compounds in E. coli makes this bacterium a very useful model system to decipher biochemical, genetic, evolutionary, and ecological aspects of the catabolism of such compounds. In the last part of the review, we discuss strategies and concepts to metabolically engineer E. coli to suit specific needs for biodegradation and biotransformation of aromatics and we provide several examples based on selected studies. Finally, conclusions derived from this review may serve as a lead for future research and applications.Keywords
This publication has 361 references indexed in Scilit:
- Crystal Structure of NAD(P)H:Flavin Oxidoreductase from Escherichia coli,Biochemistry, 1999
- Purification, Characterization, and Stereochemical Analysis of a C−C Hydrolase: 2-Hydroxy-6-keto-nona-2,4-diene-1,9-dioic Acid 5,6-HydrolaseBiochemistry, 1997
- Sequence of the Escherichia coli C homoprotocatechuic acid degradative operon completed with that of the 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase-encoding gene (hpcH)Gene, 1995
- Escherichia coli K-12 Copper-Containing Monoamine Oxidase: Investigation of the Copper Binding Ligands by Site-Directed Mutagenesis, Elemental Analysis and Topa Quinone FormationBiochemical and Biophysical Research Communications, 1995
- Sequence of the hpcC and hpcG genes of the meta-fission homoprotocatechuic acid pathway of Escherichia coli C: nearly 40% amino-acid identity with the analogous enzymes of the catechol pathwayGene, 1995
- The nucleotide sequence of the Tn5271 3-chlorobenzoate 3,4-dioxygenase genes (cbaAB) unites the class IA oxygenases in a single lineageMicrobiology, 1995
- Overproduction, purification and properties of 2,3-dihydroxyphenylpropionate 1,2-dioxygenase from EscherichiacoliBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1993
- Evolutionary divergence of pobA, the structural gene encoding p-hydroxybenzoate hydroxylase in an Acinetobacter calcoaceticus strain well-suited for genetic analysisGene, 1993
- Decarboxylation of Substituted Cinnamic Acids by Enterobacteria: the Influence on Beer FlavourJournal of Applied Bacteriology, 1975
- Enzymatic Decarboxylation of the Aminobenzoates1Journal of the American Chemical Society, 1957