Date of Award
Spring 2020
Degree Type
Thesis
Department
Chemistry and Biochemistry
Director of Thesis
Thomas Makris, PhD
First Reader
Hippokratis Kiaris, PhD
Second Reader
Hippokratis Kiaris, PhD
Abstract
The overall structure and ligand arrangement of diiron enzymes influence their function and catalytic potential, allowing for them to catalyze an expansive breadth of high energy transformations. The diiron enzyme CADD from Chlamydia trachomatis is involved in a novel biosynthetic pathway for p-aminobenzoic acid (pABA), a precursor for tetrahydrofolate. The unique ligand structure and reactivity of CADD and homolog NE1434 provide an intriguing means to contrast structure function relationships with other known diiron enzymes that activate dioxygen. In this work, studies of CADD and NE1434 orthologs and comparison to other diiron enzymes reveal several sequence motifs that are likely critical for its distinct function.
First Page
1
Last Page
26
Recommended Citation
Zambelas, Joseph M., "A Broadly Distributed, Novel Class of Diiron Enzymes Involved in Para-Aminobenzoate Synthesis" (2020). Senior Theses. 371.
https://scholarcommons.sc.edu/senior_theses/371
Rights
© 2020, Joseph M Zambelas