Observation of the pathway from lysine to the isoprenoidal lipid of halophilic archaea, Halobacterium halobium and Natrinema pallidum, using regiospecifically deuterated lysine

Noriaki Yamauchi, Satoshi Endoh, Keiko Kato, Tatsushi Murae

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4 Citations (Scopus)

Abstract

We examined the incorporation of lysine into archaeal isoprenoidal lipids of halophilic archaea, Natrinema pallidum and Halobacterium halobium using two regiospecifically deuterium-labeled derivatives, [3,3-2H2] and [6,6-2H2]lysines. The two deuterated lysines were synthesized, and the incorporation of deuterium to the lipid core was defined by 2H NMR. The results revealed that lysine is degraded to crotonoyl-CoA by the decarboxylation of carboxylate in the metabolism of halophilic archaea, much like the metabolism of lysine in aerobic bacteria; the process converts lysine to isoprenoidal lipids via the mevalonate pathway through glutaryl-CoA, crotonoyl-CoA, and acetoacetyl-CoA.

Original languageEnglish
Pages (from-to)2199-2205
Number of pages7
JournalBulletin of the Chemical Society of Japan
Volume74
Issue number11
DOIs
Publication statusPublished - Jan 1 2001

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Lysine
Lipids
Deuterium
Metabolism
Aerobic bacteria
Mevalonic Acid
Coenzyme A
Nuclear magnetic resonance
Derivatives

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

Cite this

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title = "Observation of the pathway from lysine to the isoprenoidal lipid of halophilic archaea, Halobacterium halobium and Natrinema pallidum, using regiospecifically deuterated lysine",
abstract = "We examined the incorporation of lysine into archaeal isoprenoidal lipids of halophilic archaea, Natrinema pallidum and Halobacterium halobium using two regiospecifically deuterium-labeled derivatives, [3,3-2H2] and [6,6-2H2]lysines. The two deuterated lysines were synthesized, and the incorporation of deuterium to the lipid core was defined by 2H NMR. The results revealed that lysine is degraded to crotonoyl-CoA by the decarboxylation of carboxylate in the metabolism of halophilic archaea, much like the metabolism of lysine in aerobic bacteria; the process converts lysine to isoprenoidal lipids via the mevalonate pathway through glutaryl-CoA, crotonoyl-CoA, and acetoacetyl-CoA.",
author = "Noriaki Yamauchi and Satoshi Endoh and Keiko Kato and Tatsushi Murae",
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T1 - Observation of the pathway from lysine to the isoprenoidal lipid of halophilic archaea, Halobacterium halobium and Natrinema pallidum, using regiospecifically deuterated lysine

AU - Yamauchi, Noriaki

AU - Endoh, Satoshi

AU - Kato, Keiko

AU - Murae, Tatsushi

PY - 2001/1/1

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N2 - We examined the incorporation of lysine into archaeal isoprenoidal lipids of halophilic archaea, Natrinema pallidum and Halobacterium halobium using two regiospecifically deuterium-labeled derivatives, [3,3-2H2] and [6,6-2H2]lysines. The two deuterated lysines were synthesized, and the incorporation of deuterium to the lipid core was defined by 2H NMR. The results revealed that lysine is degraded to crotonoyl-CoA by the decarboxylation of carboxylate in the metabolism of halophilic archaea, much like the metabolism of lysine in aerobic bacteria; the process converts lysine to isoprenoidal lipids via the mevalonate pathway through glutaryl-CoA, crotonoyl-CoA, and acetoacetyl-CoA.

AB - We examined the incorporation of lysine into archaeal isoprenoidal lipids of halophilic archaea, Natrinema pallidum and Halobacterium halobium using two regiospecifically deuterium-labeled derivatives, [3,3-2H2] and [6,6-2H2]lysines. The two deuterated lysines were synthesized, and the incorporation of deuterium to the lipid core was defined by 2H NMR. The results revealed that lysine is degraded to crotonoyl-CoA by the decarboxylation of carboxylate in the metabolism of halophilic archaea, much like the metabolism of lysine in aerobic bacteria; the process converts lysine to isoprenoidal lipids via the mevalonate pathway through glutaryl-CoA, crotonoyl-CoA, and acetoacetyl-CoA.

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