PMID:9109378
| Citation |
Ferrandez, A, Prieto, MA, Garcia, JL and Diaz, E (1997) Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli. FEBS Lett. 406:23-7 |
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| Abstract |
The padA gene encoding the phenylacetaldehyde dehydrogenase involved in the catabolism of 2-phenylethylamine in Escherichia coli has been cloned, sequenced, and located at 31.0 min on the chromosome. The deduced PadA polypeptide contains 499 amino acid residues with a predicted molecular mass of 53.7 kDa, and its primary structure reveals significant similarity with that of members of the aldehyde dehydrogenase superfamily. By engineering optimal transcription and translation elements, a high expression of the padA gene has been achieved. The active PadA enzyme is a homodimer that prefers NAD+ over NADP+ as coenzyme. The enzyme efficiently oxidizes only phenylacetaldehyde-like aromatic aldehydes, and has a weak esterase activity with p-nitrophenol. The padA gene constitutes a new catabolic tool for designing DNA cassettes to expand the abilities of microorganisms to degrade toxic aromatic compounds. |
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| Keywords |
Aldehyde Oxidoreductases/genetics; Amino Acid Sequence; Base Sequence; Chromosome Mapping; Chromosomes, Bacterial; Cloning, Molecular; DNA, Recombinant; Escherichia coli/enzymology; Molecular Sequence Data |
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