We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
The crystal structure of seabream antiquitin reveals the structural basis of its substrate specificity
- Authors
Tang, Wai-Kwan; Wong, Kam-Bo; Lam, Yuk-Man; Cha, Sun-Shin; Cheng, Christopher H.K.; Fong, Wing-Ping
- Abstract
Abstract: The crystal structure of seabream antiquitin in complex with the cofactor NAD+ was solved at 2.8Å resolution. The mouth of the substrate-binding pocket is guarded by two conserved residues, Glu120 and Arg300. To test the role of these two residues, we have prepared the two mutants E120A and R300A. Our model and kinetics data suggest that antiquitin’s specificity towards the substrate α-aminoadipic semialdehyde is contributed mainly by Glu120 which interacts with the α-amino group of the substrate. On the other hand, Arg300 does not have any specific interaction with the α-carboxylate group of the substrate, but is important in maintaining the active site conformation.
- Subjects
SUBSTRATES (Materials science); GENETIC mutation; AMINO group
- Publication
FEBS Letters, 2008, Vol 582, Issue 20, p3090
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2008.07.059