Human 5'-Aminolevulinate Synthase, Erythroid-Specific (ALAS2); A Target Enabling Package
Creators
- 1. Structural Genomics Consortium, Nuffield Department of Medicine, University of Oxford
- 2. Department of Biochemistry and Molecular Biology, University of Georgia, Athens GA
Description
Erythorid specific 5’-Aminolevulinate synthase (ALAS2) catalyses the first and rate-determining step in haem biosynthesis during erythroid development. This TEP provides the structural biology tools to facilitate two aspects of ALAS2 research: (i) understanding how mutations in the ALAS2 C-terminus, a region unique to higher eukaryotes, lead to over-activity of the enzyme associated with a gain-of-function disorder; and (ii) providing chemical starting points to explore metabolic intervention of ALAS2, as substrate reduction therapy for the group of porphyria disorders that are associated with haem biosynthetic steps downstream of ALAS2.
Notes
Files
ALAS2_TEP.pdf
Files
(483.7 kB)
Name | Size | Download all |
---|---|---|
md5:08e1bd8e868e93f3f0db70b639d19aeb
|
483.7 kB | Preview Download |
Additional details
Related works
- Is part of
- https://www.thesgc.org/tep (URL)
Funding
- A UK Hub to Catalyse Open Target Discovery. 106169
- Wellcome Trust