Premium
Enzymatic synthesis of isotopically labelled serine and tryptophan for application in peptide synthesis
Author(s) -
Malthouse J. Paul G.,
Fitzpatrick Teresa B.,
Milne John J.,
Grehn Leif,
Ragnarsson Ulf
Publication year - 1997
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/(sici)1099-1387(199709)3:5<361::aid-psc112>3.0.co;2-o
Subject(s) - serine hydroxymethyltransferase , serine , isotopomers , chemistry , tryptophan synthase , tryptophan , glycine , enzyme , chromatography , biochemistry , amino acid , organic chemistry , molecule
L‐[1,2‐ 13 C 2 , 15 N]Serine was prepared from [1,2‐ 13 C 2 , 15 N]glycine on a gram scale by the use of the enzyme serine hydroxymethyltransferase. The reaction was monitored by 13 C‐NMR spectroscopy. This is the first simultaneously 13 C‐ and 15 N‐labelled serine isotopomer so far reported. Part of the product was directly converted by tryptophan synthase to L‐[1,2‐ 13 C 2 , 15 N]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. © 1997 European Peptide Society and John Wiley & Sons, Ltd. J. Pep. Sci. 3: 361–366 No. of Figures: 1. No. of Tables: 0. No. of References: 32