Neurochemical Research

, Volume 28, Issue 6, pp 797–803

Cloning and Expression of Human Placental L-Dopa Decarboxylase

Authors

  • Maria-Zaharenia Siaterli
    • Department of Biochemistry and Molecular Biology, PanepistimiopolisUniversity of Athens
    • Department of Biochemistry and Molecular Biology, PanepistimiopolisUniversity of Athens
  • Emmanuel G. Fragoulis
    • Department of Biochemistry and Molecular Biology, PanepistimiopolisUniversity of Athens
Article

DOI: 10.1023/A:1023246620276

Cite this article as:
Siaterli, M., Vassilacopoulou, D. & Fragoulis, E.G. Neurochem Res (2003) 28: 797. doi:10.1023/A:1023246620276

Abstract

L-Dopa decarboxylase (DDC) is a pyridoxal 5-phosphate (PLP)-dependent enzyme that catalyses the decarboxylation of L-Dopa to dopamine. In this study we show the expression of DDC in human placental tissue and present data on the molecular cloning and in vitro expression of the active recombinant enzyme. Our analyses indicated the presence of both alternative DDC mRNA splice variants (neuronal and nonneuronal) in human placenta. Cloning of the coding region of the DDC cDNA into the pTrcHisA expression vector led to the production of the enzymatically active recombinant protein. The obtained recombinant enzyme specific activity values were in good agreement with the results obtained for the purified enzyme from human kidney. The availability of active recombinant human DDC could provide information leading to the better understanding of the enzyme's structure and substrate specificity, as well as its regulation and involvement in pathological conditions.

L-Dopa decarboxylasehuman placentarecombinant enzymealternative splicing5′ UTR
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Copyright information

© Plenum Publishing Corporation 2003