Characterization of 3-isopropylmalate dehydrogenase from extremely halophilic archaeon Haloarcula japonica

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 in...

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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2021-08, Vol.85 (9), p.1986-1994
Hauptverfasser:	Nagaoka, Shintaro, Sugiyama, Noriko, Yatsunami, Rie, Nakamura, Satoshi
Format:	Artikel
Sprache:	eng
Schlagworte:	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
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Zusammenfassung:	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.
ISSN:	1347-6947 1347-6947
DOI:	10.1093/bbb/zbab122