Expression, purification and preliminary crystallographic studies of NahF, a salicylaldehyde dehydrogenase from Pseudomonas putida G7 involved in naphthalene degradation.

@article{Coitinho2012ExpressionPA,
  title={Expression, purification and preliminary crystallographic studies of NahF, a salicylaldehyde dehydrogenase from Pseudomonas putida G7 involved in naphthalene degradation.},
  author={Juliana Barbosa Coitinho and D{\'e}bora Maria Abrantes Costa and Samuel Leite Guimar{\~a}es and Alfredo Miranda de G{\'o}es and Ronaldo Alves Pinto Nagem},
  journal={Acta crystallographica. Section F, Structural biology and crystallization communications},
  year={2012},
  volume={68 Pt 1},
  pages={93-7}
}
Pseudomonas putida G7 is one of the most studied naphthalene-degrading species. The nah operon in P. putida, which is present on the 83 kb metabolic plasmid NAH7, codes for enzymes involved in the conversion of naphthalene to salicylate. The enzyme NahF (salicylaldehyde dehydrogenase) catalyzes the last reaction in this pathway. The nahF gene was subcloned into the pET28a(TEV) vector and the recombinant protein was overexpressed in Escherichia coli Arctic Express at 285 K. The soluble protein… CONTINUE READING
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