Molecular cloning and homology modeling of protocatechuate 3,4-dioxygenase from Pseudomonas marginata

Evamaria I. Petersen, Johannes Zuegg, Douglas W. Ribbons, Helmut Schwab*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

11 Citations (Scopus)


The genes that encode the α and β subunits of protocatechuate 3,4-dioxygenase (3,4-PCD [EC]) were cloned from a Pseudomonas marginata genomic library. These genes pcaG and pcaH, were found when screening the library for hydrolase genes. The two open reading frames of the PCD genes could be identified adjacent to an esterase gene by sequence homology. A 1.7-kb KpnI/ApaI fragment, carrying pcaG and pcaH, was subcloned and the genes were functionally expressed in Escherichia coli. The deduced amino acid sequence shows high homology to previously determined amino acid sequences of bacterial protocatechuate 3,4-dioxygenases. A homology model based on the available crystal structure of the protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa shows high similarity with the binding and catalytic sites.

Original languageEnglish
JournalMicrobiological Research
Issue number4
Pages (from-to)359-370
Number of pages12
Publication statusPublished - Dec 1996


  • 3D structure modeling
  • Molecular cloning
  • Nucleotide sequence
  • Protocatechuate 3,4-dioxygenase
  • Pseudomonas marginata


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