Date of Award
5-7-2016
Degree Type
Thesis
Degree Name
Master of Science (MS)
Department
Chemistry
First Advisor
Aimin Liu
Second Advisor
Giovanni Gadda
Third Advisor
Donald Hamelberg
Abstract
In 2007, a gene homolog of CDO encoded by the gene Gm237 in the DUF164 family was identified as cysteamine dioxygenase (ADO). ADO is one of the only known thiol dioxygenases found in mammals. Both ADO and its partner cysteine dioxygenase (CDO) are non-heme iron dependent enzymes that play a crucial role in the biosynthesis of taruine/hypotaurine by insertion of a dioxygen molecule. However, ADO has been overshadowed by CDO as heavy research focus on CDO over the past decade has led to the elucidation of its structure and possible mechanistic properties. In an effort to further understand ADO’s mechanism and regulating role in vivo, this work will be focused on the mammalian hADO and trying to gain further insight on hADO’s structural features via crystallography work. Investigation of the crystallization parameters for hADO has elucidated several potential conditions. Detailed work on these crystallization parameters will be presented.
DOI
https://doi.org/10.57709/8517965
Recommended Citation
Xiong, Tseng and Xiong, Tseng, "Investigation Of A Novel Mammalian Thiol Dioxygenase Structure: Human Cysteamine Dioxygenase." Thesis, Georgia State University, 2016.
doi: https://doi.org/10.57709/8517965