SIRT5 mutants reveal the role of conserved asparagine and glutamine residues in the NAD+-binding pocket

Takeshi Yokoyama*, Yuki Takayama, Mineyuki Mizuguchi, Yuko Nabeshima, Katsuhiro Kusaka

*この論文の責任著者

研究成果: ジャーナルへの寄稿学術論文査読

抄録

SIRT5, one of the mammalian sirtuins, specifically recognizes succinyl-lysine residues on proteins and catalyzes the desuccinylation reaction. In this study, we characterized SIRT5 mutants with hydrophobic amino acid substitutions at Q140 and N141, in addition to the catalytic residue H158, known as an active site residue, by the Michaelis–Menten analysis and X-ray crystallography. Kinetic analysis showed that the catalytic efficiency (kcat/Km) of the Q140L and N141V mutants decreased to 0.02 times and 0.0038 times that of the wild-type SIRT5, respectively, with the activity of the N141V mutant becoming comparable to that of the H158M mutant. Our findings indicate that N141 contributes significantly to the desuccinylation reaction.

本文言語英語
ページ(範囲)2269-2280
ページ数12
ジャーナルFEBS Letters
598
18
DOI
出版ステータス出版済み - 2024/09

ASJC Scopus 主題領域

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

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