Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli

FEBS Letters

Garcı́a, José L.¹  Dı́az, Eduardo¹  Prieto, Marı́a A.¹  Ferrández, Abel¹ 

[1] Departamento de Microbiologı́a Molecular, Centro de Investigaciones Biológicas, CSIC, Velázquez 144, 28006 Madrid, Spain

关键词: Phenylacetaldehyde dehydrogenase;    Gene expression;    Escherichia coli;    Catabolism;    Primary structure;    PAL;    phenylacetaldehyde;    PA;    phenylacetic acid;   

DOI  :  10.1016/S0014-5793(97)00228-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown