In:
Bioscience, Biotechnology, and Biochemistry, Informa UK Limited, Vol. 85, No. 9 ( 2021-08-25), p. 1986-1994
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.
Type of Medium:
Online Resource
ISSN:
1347-6947
Language:
English
Publisher:
Informa UK Limited
Publication Date:
2021
detail.hit.zdb_id:
2110940-0
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