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Gene Review

pcaD  -  3-oxoadipate enol-lactonase

Acinetobacter sp. ADP1

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Disease relevance of pcaD


High impact information on pcaD

  • Sequence repetitions within pcaD suggest that the multiple mutations required for its extensive divergence from catD were achieved in part by acquisition of a complex DNA slippage structure [1].
  • This report presents the 2754-nucleotide (nt) sequence of a HindIII restriction fragment containing pcaD, the 801-bp gene encoding beta-ketoadipate enol-lactone hydrolase I [1].
  • When the mutation was incorporated into the A. tumefaciens chromosome, it eliminated expression of the pcaD gene and at least three other pca genes as well [2].
  • Mutants selected on this medium contained the original mutation in pcaD and also carried spontaneous mutations in pobA [4].
  • Mutations in pcaD prevented growth of A. calcoaceticus with succinate in the presence of p-hydroxybenzoate [4].

Chemical compound and disease context of pcaD


Biological context of pcaD

  • In the 56% of the genes where selection for identical aa residues was not imposed, pcaD and catD have diverged so extensively that nt sequence identity of the aligned segments is only 28.2%; the G+C contents of these segments from the respective genes differ by 8% [1].
  • The recombinant plasmid, pAN1, complemented P. putida mutants with lesions in catB, catC, pcaD, and pcaE genes; the complemented activities were expressed constitutively in the recombinant P. putida strains [5].


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