Title page for ETD etd-08262010-121034

Type of Document Master's Thesis
Author Aljabri, Hareb Mohammed
Author's Email Address haljabri@vt.edu
URN etd-08262010-121034
Title Comparative analysis of Anopheles gambiae L-tyrosine decarboxylase and L-DOPA decarboxylase
Degree Master of Science In the Life Sciences
Department Biochemistry
Advisory Committee
Advisor Name Title
Li, Jianyong Committee Chair
Larson, Timothy J. Committee Member
Tu, Zhijian Jake Committee Member
  • Tyrosine
  • DOPA decarboxylase (DDC)
  • Tyrosine decarboxylase (TDC)
  • Tyramine
  • Dopamine
Date of Defense 2010-08-16
Availability unrestricted
A major pathway of tyramine and dopamine synthesis in insects is through the decarboxylation of tyrosine and DOPA, respectively. Although tyrosine decarboxylase (TDC) has been mentioned in some reports, it has never been critically analyzed. The high sequence identity shared by tyrosine decarboxylase and DOPA decarboxylase in insects, and the similar structures of the substrates, tyrosine and DOPA, raise the possibility that both tyrosine decarboxylase and DOPA decarboxylase (DDC) have activities to tyrosine and DOPA. In this study, after tyrosine decarboxylase and DOPA decarboxylase enzymes of Anopheles gambiae were expressed, their substrate specificities and biochemical properties were critically analyzed. My results provide clear biochemical evidence establishing that the mosquito tyrosine decarboxylase functions primarily on the production of tyramine with low activity to DOPA. In contrast, mosquito DOPA decarboxylase is highly specific to DOPA with essentially no activity to tyrosine.
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