The crystal structure of seabream antiquitin reveals the structural basis of its substrate specificity SCIE SCOPUS

Cited 16 time in WEB OF SCIENCE Cited 16 time in Scopus
Title
The crystal structure of seabream antiquitin reveals the structural basis of its substrate specificity
Author(s)
Tang, Wai-Kwan; Wong, Kam-Bo; Lam, Yuk-Man; Cha, Sun-Shin; Cheng, Christopher H. K.; Fong, Wing-Ping
Publication Year
2008-09-03
Abstract
The crystal structure of seabream antiquitin in complex with the cofactor NAD(+) was solved at 2.8 angstrom 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 alpha-aminoadipic semialdehyde is contributed mainly by Glu120 which interacts with the alpha-amino group of the substrate. On the other hand, Arg300 does not have any specificity interaction with the alpha-carboxylate group of the substrate, but is important in maintaining the active site conformation. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
ISSN
0014-5793
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/4450
DOI
10.1016/j.febslet.2008.07.059
Bibliographic Citation
FEBS LETTERS, v.582, no.20, pp.3090 - 3096, 2008
Publisher
WILEY
Subject
TURGOR-RESPONSIVE GENE; ALDEHYDE-DEHYDROGENASE; MOLECULAR-CLONING; PROTEIN; EXPRESSION; LIVER; IDENTIFICATION; PURIFICATION; SUPERFAMILY; ARABIDOPSIS
Keywords
antiquitin; ALDH7; alpha-aminoadipic semialdehyde; x-ray crystallography; site-directed mutagenesis; pyridoxine-dependent epilepsy
Type
Article
Language
English
Document Type
Article
Publisher
WILEY
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