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Scientific article
English

Enzymatic synthesis of isotopically labelled serine and tryptophan for application in peptide synthesis

Published inJournal of peptide science, vol. 3, no. 5, p. 361-366
Publication date1997
Abstract

L-[1.2-13C2, 15N]Serine was prepared from [1,2-13C2, 15N]glycine on a gram scale by the use of the enzyme serine hydroxymethyltransferase. The reaction was monitored by 13C-NMR spectroscopy. This is the first simultaneously 13C- and 15N-labelled serine isotopomer so far reported. Part of the product was directly converted by tryptophan synthase to L-[1,2-13C2, 15N]tryptophan which could conveniently be purified and isolated as Boc-derivative in a yield of 71%. Most of the serine was isolated similarly but to remove remaining starting material in this case purification by column chromatography was required.

Keywords
  • Carbon Isotopes
  • Glycine Hydroxymethyltransferase/metabolism
  • Magnetic Resonance Spectroscopy
  • Nitrogen Isotopes
  • Serine/chemistry/metabolism
  • Tryptophan/chemistry/metabolism
  • Tryptophan Synthase/metabolism
Affiliation Not a UNIGE publication
Citation (ISO format)
MALTHOUSE, J P et al. Enzymatic synthesis of isotopically labelled serine and tryptophan for application in peptide synthesis. In: Journal of peptide science, 1997, vol. 3, n° 5, p. 361–366. doi: 10.1002/(SICI)1099-1387(199709)3:5<361::AID-PSC112>3.0.CO;2-O
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Article (Published version)
accessLevelRestricted
ISSN of the journal1075-2617
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