Type
Text
Type
Thesis
Advisor
Glynn, Steven. | French, Jarrod B
Date
2014-12-01
Keywords
Biochemistry | adenylosuccinate lyase, purinosome
Department
Department of Biochemistry and Cell Biology.
Language
en_US
Source
This work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree.
Identifier
http://hdl.handle.net/11401/76927
Publisher
The Graduate School, Stony Brook University: Stony Brook, NY.
Format
application/pdf
Abstract
Cells require purines for critical biological processes that can be created by the de novo biosynthetic pathway or maintained by the salvage pathways. The de novo pathway in humans requires 6 enzymes, some of which are multifunctional. Adenylosuccinate lyase (ASL) catalyzes step 8 of the de novo pathway converting susuccinylaminoimidazolecarboxamide ribonucleotide (SAICAR) to aminoimidazolecarboxamide ribotide (AICAR). It also catalyzes the second step of the purine nucleotide cycle by converting SAMP to AMP. A short isoform of ASL (sASL) is ubiquitously expressed in all cell types at a lower concentration. This shortened splice variant does not perform catalysis on either of the aforementioned substrates. It has been suggested that sASL may play an important structural role in the formation and stabilization of the purinosome assembly. The purpose of this work is to characterize the short isoform of ASL and elucidate its structure and function. To date, I have cloned sASL, expressed and purified the protein, and identified a buffer that stabilizes it. | 48 pages
Recommended Citation
Rajan, Benjamin, "Expression, Purification, and Characterization of the Short Isoform of Adenylosuccinate Lyase" (2014). Stony Brook Theses and Dissertations Collection, 2006-2020 (closed to submissions). 2800.
https://commons.library.stonybrook.edu/stony-brook-theses-and-dissertations-collection/2800