Genetic characterization of the phenylacetyl-coenzyme A oxygenase from the aerobic phenylacetic acid degradation pathway of Escherichia coli

Article Abstract:

The paaABCDE genes of the paa cluster responsible for phenylacetate degradation in Escherichia coli W encode a five-component oxygenase that hydroxylates phenylacetyl-coenzyme A (CoA), the first intermediate of the pathway. The primary structure of the subunits of bacterial phenylacetyl-CoA oxygenases revealed that these enzymes constitute the prototype of a new and distinct group of the large bacterial diiron multicomponent oxygenase family.

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Biodegradation of aromatic compounds by Escherichia coli

Article Abstract:

Research findings demonstrate that Escherichia coli is capable of catabolizing aromatic compounds and it possesses the genetic make--up and the aromatic ring-hydroxylating dioxygenases. The regulatory proteins and promoters involved in the expression of catabolic genes of the aromatic pathways show structural and functional diversity.

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In vivo immobilization of fusion proteins on bioplastics by the novel Tag BioF

Article Abstract:

Bioplastics also known as Polyhydroxyalkanoates (PHAs) are biodegradable polymers produced by bacteria found in cytoplasm. Based on these bioplastics, a new immobilization system is developed which is discussed with illustrations.

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