Characterization of 3-isopropylmalate dehydrogenase from extremely halophilic archaeon Haloarcula japonica-Reference-Cited by-同舟云学术

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

Published:2021-07-02 Issue:9 Volume:85 Page:1986-1994
ISSN:1347-6947
Container-title:Bioscience, Biotechnology, and Biochemistry
language:en
Short-container-title:

Author:

Nagaoka Shintaro¹,Sugiyama Noriko¹,Yatsunami Rie¹,Nakamura Satoshi¹²

Affiliation:

1. School of Life Science and Technology, Tokyo Institute of Technology, Midori-ku, Yokohama, Japan

2. National Institute of Technology (KOSEN), Numazu College, Numazu, Shizuoka, Japan

Abstract

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.

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

Link

http://academic.oup.com/bbb/advance-article-pdf/doi/10.1093/bbb/zbab122/39568956/zbab122.pdf

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