Parasitology Research

, Volume 109, Issue 4, pp 1065–1074 | Cite as

Cloning and characterization of a novel enzyme: tyrosine hydroxylase from Schistosoma japonicum

  • Yuansheng Hu
  • Dujuan Shi
  • Qingli Luo
  • Qingzhong Liu
  • Yindi Zhou
  • Lili Liu
  • Li Yu
  • Wei Wei
  • Jilong Shen
Original Paper
First Online:
Received:
Accepted:

Abstract

Catecholamines, such as dopamine and noradrenaline, play important roles as neuromuscular transmitters and modulators in all parasitic helminthes, including Schistosoma japonicum. S. japonicum tyrosine hydroxylase (SjTH) was amplified by rapid amplification of cDNA ends polymerase chain reaction that shows strong homology to Schistosoma mansoni tyrosine hydroxylase, the enzyme that catalyzes the first and rate-limiting step in the biosynthesis of catecholamines. The SjTH transcripts encoded the protein of 463 amino acids and a predicted size of 54 kDa. Purified recombinant SjTH as an N-terminal histidine fusion protein expressed in Escherichia coli showed catalytic activity that was confirmed with 3H tyrosine uptake. The purified enzyme was found to have the same absolute requirement for a tetrahydrobiopterin cofactor and similar sensitivity to be inhibited by high concentration of the substrate, tyrosine, as the mammalian enzyme. Also, purified SjTH showed characteristic inhibition by catecholamine products. The phosphorylated peptide from SjTH could interact with Sj14-3-3 signal protein. This evidence indicates that SjTH encodes a functional tyrosine hydroxylase that has catalytic properties similar to those of the mammalian hosts' enzyme, and its catalytic activity could be regulated by a phosphorylated or dephosphorylated form. This demonstration of SjTH further suggests that the parasites have the enzymatic capacity to synthesize catecholamines endogenously.

Keywords

Tyrosine Hydroxylase Adult Worm Tryptophan Hydroxylase Schistosoma Japonicum Mammalian Enzyme 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Notes

Acknowledgments

This work was funded by NSFC (No. 30872210), NSFAnhui (No. 090413089), NSF Anhui of Higher Education (No. KJ2007A030 and No. KJ2008B19ZC), and research fund for Doctoral Programme of higher education of China (No.00803660003).

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Copyright information

© Springer-Verlag 2011

Authors and Affiliations

  • Yuansheng Hu
    • 1
    • 2
    • 3
  • Dujuan Shi
    • 2
    • 3
  • Qingli Luo
    • 2
  • Qingzhong Liu
    • 4
  • Yindi Zhou
    • 3
  • Lili Liu
    • 2
  • Li Yu
    • 2
  • Wei Wei
    • 1
  • Jilong Shen
    • 1
    • 2
  1. 1.Institute of Clinical PharmacologyAnhui Medical University, The Key Laboratories of Zoonoses and Pathogen Biology, AnhuiHefeiChina
  2. 2.Anhui Key Laboratories of Zoonoses and Pathogen BiologyHefeiChina
  3. 3.Department of Clinical LaboratoryThe Third Affiliated Hospital of Anhui Medical UniversityHefeiChina
  4. 4.Department of Clinical LaboratoryThe First Affiliated Hospital of Wenzhou Medical UniversityWenzhouChina

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