Carbon-skeleton rearrangement of an amino acid derivative as mediated by hydrophobic vitamin B 12 covalently bound to a lipid species in a bilayer membrane

Yukito Murakami, Yoshio Hisaeda, Akihiro Ogawa, Teruhisa Ohno

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Diethyl 2-acetylamino-2-methylpropanedioate co-ordinated to a hydrophobic vitamin B 12 covalently bound to a peptide lipid underwent a carbon-skeleton rearrangement to afford diethyl 2-acetylaminobutanedioate in the single-walled vesicle of N,N-bis(hexadecyl)-Nα-(6-sulfohexanoyl)-L- alaninamide under photolysis conditions.

Original languageEnglish
Pages (from-to)189-191
Number of pages3
JournalJournal of the Chemical Society, Perkin Transactions 2
Issue number2
Publication statusPublished - Dec 1 1995

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Photolysis
Vitamin B 12
Carbon
Derivatives
Membranes
Lipids
Amino Acids
Peptides

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

Cite this

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abstract = "Diethyl 2-acetylamino-2-methylpropanedioate co-ordinated to a hydrophobic vitamin B 12 covalently bound to a peptide lipid underwent a carbon-skeleton rearrangement to afford diethyl 2-acetylaminobutanedioate in the single-walled vesicle of N,N-bis(hexadecyl)-Nα-(6-sulfohexanoyl)-L- alaninamide under photolysis conditions.",
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AU - Murakami, Yukito

AU - Hisaeda, Yoshio

AU - Ogawa, Akihiro

AU - Ohno, Teruhisa

PY - 1995/12/1

Y1 - 1995/12/1

N2 - Diethyl 2-acetylamino-2-methylpropanedioate co-ordinated to a hydrophobic vitamin B 12 covalently bound to a peptide lipid underwent a carbon-skeleton rearrangement to afford diethyl 2-acetylaminobutanedioate in the single-walled vesicle of N,N-bis(hexadecyl)-Nα-(6-sulfohexanoyl)-L- alaninamide under photolysis conditions.

AB - Diethyl 2-acetylamino-2-methylpropanedioate co-ordinated to a hydrophobic vitamin B 12 covalently bound to a peptide lipid underwent a carbon-skeleton rearrangement to afford diethyl 2-acetylaminobutanedioate in the single-walled vesicle of N,N-bis(hexadecyl)-Nα-(6-sulfohexanoyl)-L- alaninamide under photolysis conditions.

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JO - Journal of the Chemical Society, Perkin Transactions 2

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