The pathway of leucine to mevalonate in halophilic archaea: Efficient incorporation of leucine into isoprenoidal lipid with the involvement of isovaleryl-CoA dehydrogenase in halobacterium salinarum

Noriaki Yamauchi

doi:10.1271/bbb.90814

The pathway of leucine to mevalonate in halophilic archaea: Efficient incorporation of leucine into isoprenoidal lipid with the involvement of isovaleryl-CoA dehydrogenase in halobacterium salinarum

Noriaki Yamauchi

Material Science of Solar Planets

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9 Citations (Scopus)

Abstract

The pathway of leucine to mevalonate, which has attracted attention in the study of the biosynthesis of isoprenoid in parasitic protozoa and myxobacterium, was observed in the biosynthesis of the lipid core in halophilic archaea. The involvement of isovaleryl-CoA dehydrogenase was strongly suggested, with stereospecific conversion of the diastereotopic methyl group of leucine to isoprenoidal lipid.

Original language	English
Pages (from-to)	443-446
Number of pages	4
Journal	Bioscience, Biotechnology and Biochemistry
Volume	74
Issue number	2
DOIs	https://doi.org/10.1271/bbb.90814
Publication status	Published - Mar 1 2010

All Science Journal Classification (ASJC) codes

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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The pathway of leucine to mevalonate in halophilic archaea: Efficient incorporation of leucine into isoprenoidal lipid with the involvement of isovaleryl-CoA dehydrogenase in halobacterium salinarum. / Yamauchi, Noriaki.
In: Bioscience, Biotechnology and Biochemistry, Vol. 74, No. 2, 01.03.2010, p. 443-446.

Research output: Contribution to journal › Article › peer-review

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The pathway of leucine to mevalonate in halophilic archaea: Efficient incorporation of leucine into isoprenoidal lipid with the involvement of isovaleryl-CoA dehydrogenase in halobacterium salinarum

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