1. Biochemical characterization of archaeal homocitrate synthase from Sulfolobus acidocaldarius.
- Author
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Suzuki T, Akiyama N, Yoshida A, Tomita T, Lassak K, Haurat MF, Okada T, Takahashi K, Albers SV, Kuzuyama T, and Nishiyama M
- Subjects
- Archaeal Proteins chemistry, Archaeal Proteins genetics, Binding Sites, Lysine metabolism, Mutation, Oxo-Acid-Lyases chemistry, Oxo-Acid-Lyases genetics, Protein Binding, Archaeal Proteins metabolism, Oxo-Acid-Lyases metabolism, Sulfolobus acidocaldarius enzymology
- 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., (© 2019 Federation of European Biochemical Societies.)
- Published
- 2020
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