Reference - Detail
| RRC ID | 71021 |
|---|---|
| Author | Nagaoka S, Sugiyama N, Yatsunami R, Nakamura S. |
| Title | Characterization of 3-isopropylmalate dehydrogenase from extremely halophilic archaeon Haloarcula japonica. |
| Journal | Biosci Biotechnol Biochem |
| Abstract |
3-Isopropylmalate dehydrogenase (IPMDH) catalyzes oxidative decarboxylation of (2R, 3S)-3-isopropylmalate to 2-oxoisocaproate in leucine biosynthesis. In this study, recombinant IPMDH (HjIPMDH) from an extremely halophilic archaeon, Haloarcula japonica TR-1, was characterized. Activity of HjIPMDH increased as KCl concentration increased, and the maximum activity was observed at 3.0 m KCl. Analytical ultracentrifugation revealed that HjIPMDH formed a homotetramer at high KCl concentrations, and it dissociated to a monomer at low KCl concentrations. Additionally, HjIPMDH was thermally stabilized by higher KCl concentrations. This is the first report on haloarchaeal IPMDH. |
| Volume | 85(9) |
| Pages | 1986-1994 |
| Published | 2021-8-25 |
| DOI | 10.1093/bbb/zbab122 |
| PII | 6313295 |
| PMID | 34215877 |
| MeSH | 3-Isopropylmalate Dehydrogenase / chemistry 3-Isopropylmalate Dehydrogenase / metabolism* Amino Acid Sequence Archaeal Proteins / metabolism* Biopolymers / chemistry Genome, Archaeal Halobacteriales / enzymology* Halobacteriales / genetics Hydrogen-Ion Concentration Potassium Chloride / analysis Temperature |
| Resource | |
| General Microbes | JCM7785 |