Molecular characterization of an inducible p-coumaric acid decarboxylase from Lactobacillus plantarum: gene cloning, transcriptional analysis, overexpression in Escherichia coli, purification, and characterization

Article Abstract:

Polymerase chain reaction amplification and transcriptional analysis were utilized to determine the N-terminal amino acid sequence of the gene that encodes a Lactobacillus plantarum p-coumaric acid decarboxylase (PDC). Purification and characterization of the recombinant PDC in Escherichia coli indicated the homotetrameric character of the enzyme. The recombinant enzyme was also composed of four 23.5-kDa units with a molecular mass of 93 kDa. Furthermore, the expression of the gene was transcriptionally regulated by PDC.

Genetic aspects, Genetic regulation, Genetic transcription, Transcription (Genetics)

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Knockout of the p-coumarate decarboxylase gene from Lactobacillus plantarum reveals the existence of two other inducible enzymatic activities involved in phenolic acid metabolism

Article Abstract:

Researcher describe two acid phenol decarboxylase enzymes from Lactobacillus plantarum NC8 that are better induced by ferulic acid and glucose than by p-coumaric acid. The p-coumaric acid decarboxylase confers a selective advantage when the organism is grown in media containing p-coumaric acid.

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Expression in Escherichia coli of native and chimeric phenolic acid decarboxylases with modified enzymatic activities and method for screening recombinant E. coli strains expressing these enzymes

Article Abstract:

The C-terminal region of bacterial phenolic acid decarboxylases determines the substrate specificity of the enzyme. This was the conclusion of researchers who studied the enzyme from Lactobacillus plantarum, Pediococcus pentosaceus, Bacillus subtilis, and Bacillus pumilus.

Enzymes, Enzyme structure-activity relationships

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