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Biochemical characterization of archaeal homocitrate synthase from Sulfolobus acidocaldarius.
Suzuki, Tomohiro; Akiyama, Nagisa; Yoshida, Ayako; Tomita, Takeo; Lassak, Kerstin; Haurat, Maria Florencia; Okada, Takuya; Takahashi, Kento; Albers, Sonja-Verena; Kuzuyama, Tomohisa; Nishiyama, Makoto.
Affiliation
  • Suzuki T; Biotechnology Research Center, The University of Tokyo, Japan.
  • Akiyama N; Biotechnology Research Center, The University of Tokyo, Japan.
  • Yoshida A; Biotechnology Research Center, The University of Tokyo, Japan.
  • Tomita T; Biotechnology Research Center, The University of Tokyo, Japan.
  • Lassak K; Collaborative Research Institute for Innovative Microbiology, The University of Tokyo, Japan.
  • Haurat MF; Molecular Biology of Archaea, Institute of Biology, University of Freiburg, Germany.
  • Okada T; Molecular Biology of Archaea, Institute of Biology, University of Freiburg, Germany.
  • Takahashi K; Biotechnology Research Center, The University of Tokyo, Japan.
  • Albers SV; Biotechnology Research Center, The University of Tokyo, Japan.
  • Kuzuyama T; Molecular Biology of Archaea, Institute of Biology, University of Freiburg, Germany.
  • Nishiyama M; Biotechnology Research Center, The University of Tokyo, Japan.
FEBS Lett ; 594(1): 126-134, 2020 01.
Article in En | MEDLINE | ID: mdl-31330039
ABSTRACT
The hyperthermophilic archaeon, Sulfolobus, synthesizes lysine via the α-aminoadipate pathway; however, the gene encoding homocitrate synthase, the enzyme responsible for the first and committed step of the pathway, has not yet been identified. In the present study, we identified saci_1304 as the gene encoding a novel type of homocitrate synthase fused with a Regulation of Amino acid Metabolism (RAM) domain at the C terminus in Sulfolobus acidocaldarius. Enzymatic characterization revealed that Sulfolobus homocitrate synthase was inhibited by lysine; however, the mutant enzyme lacking the RAM domain was insensitive to inhibition by lysine. The present results indicated that the RAM domain is responsible for enzyme inhibition.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Sulfolobus acidocaldarius / Archaeal Proteins / Oxo-Acid-Lyases Language: En Journal: FEBS Lett Year: 2020 Document type: Article Affiliation country:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Sulfolobus acidocaldarius / Archaeal Proteins / Oxo-Acid-Lyases Language: En Journal: FEBS Lett Year: 2020 Document type: Article Affiliation country: