Date of Award
1-1967
Document Type
Thesis
Degree Name
Master of Science (MS)
Department
Biochemistry
First Advisor
Risinger, G. E.
Abstract
The mechanism of the dimerization of farnesyl pyrophosphate to squalene was investigated in detail. Thiamine was found to catalyze this dimerization in yeast-soluble enzyme preparations. Removal of thiamine was found to cause the buildup of farnesyl pyrophosphate in the enzyme system. Derivatives of thiamine were tested to examine their effect on the dimerization reaction and were found to be inactive. It was found that extremely small amounts of thiamine enhance the formation of squalene while large concentrations inhibit the formation of squalene. Thiamine derivatives were synthesized to try to identify the intermediates in the enzyme system. These compounds are discussed as to their relationship to the dimerization reaction. The possible involvement of thiamine in other biochemical reactions was discussed in light of the above results. Several hypothetical mechanisms were postulated to explain the systems discussed.
Recommended Citation
Durst, Horatio D., "On the mechanism of the thiamine catalyzed reductive dimerization of farnesyl pyrophosphate to squalene." (1967). LSU Historical Dissertations and Theses. 8212.
https://repository.lsu.edu/gradschool_disstheses/8212
DOI
10.31390/gradschool_disstheses.8212