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

Wai Kwan Tang, Kam Bo Wong, Yuk Man Lam, Sun Shin Cha, Christopher H.K. Cheng, Wing Ping Fong

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

The crystal structure of seabream antiquitin in complex with the cofactor NAD+ was solved at 2.8 Å 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.

Original languageEnglish
Pages (from-to)3090-3096
Number of pages7
JournalFEBS Letters
Volume582
Issue number20
DOIs
StatePublished - 3 Sep 2008

Bibliographical note

Funding Information:
This work was supported by a grant from the Research Grants Council of the Hong Kong Special Administrative Region (Project No. 464407). Work performed at KORDI was supported by the Marine & Extreme Genome Research Center Program, Ministry of Land, Transport, and Maritime Affairs, Republic of Korea.

Keywords

  • ALDH7
  • Antiquitin
  • Pyridoxine-dependent epilepsy
  • Site-directed mutagenesis
  • X-ray crystallography
  • α-Aminoadipic semialdehyde

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